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Protein Page:
TXN (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TXN 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. Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. In case of infection, interacts with S.typhimurium protein slrP. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA- binding activity in a redox-dependent manner. Up-regulated by ionizing radiation. Belongs to the thioredoxin family. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 9q31
Cellular Component: cytoplasm; cytosol; mitochondrion; nucleoplasm; nucleus
Molecular Function: oxidoreductase activity, acting on sulfur group of donors, disulfide as acceptor; peptide disulfide oxidoreductase activity; protein binding; protein disulfide oxidoreductase activity
Biological Process: activation of protein kinase B; cell motility; cell proliferation; cell redox homeostasis; cell-cell signaling; cellular protein metabolic process; gene expression; glycerol ether metabolic process; innate immune response; negative regulation of protein export from nucleus; negative regulation of transcription from RNA polymerase II promoter; nucleobase, nucleoside and nucleotide interconversion; nucleobase, nucleoside and nucleotide metabolic process; positive regulation of DNA binding; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein kinase B signaling cascade; protein folding; protein repair; regulation of protein import into nucleus, translocation; response to radiation; response to reactive oxygen species; signal transduction; sulfate assimilation; transcription initiation from RNA polymerase II promoter
Reference #:  P10599 (UniProtKB)
Alt. Names/Synonyms: ADF; ATL-derived factor; DKFZp686B1993; MGC61975; SASP; Surface-associated sulphydryl protein; THIO; Thioredoxin; TRDX; TRX; TRX1; TXN
Gene Symbols: TXN
Molecular weight: 11,737 Da
Basal Isoelectric point: 4.82  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TXN

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: T100‑p
intracellular localization: T100‑p

Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 K3‑ac _____MVkQIESktA
0 3 K8 MVkQIESKtAFQEAL
0 2 K8‑ub MVkQIESktAFQEAL
0 1 K8‑sc MVkQIESktAFQEAL
0 1 T9‑p VkQIESktAFQEALD
0 13 K39‑ac CGPCKMIkPFFHsLs
0 4 K39‑ub CGPCKMIkPFFHsLs
0 1 K39‑sc CGPCKMIkPFFHsLs
0 2 S44‑p MIkPFFHsLsEKYSN
0 1 S46‑p kPFFHsLsEKYSNVI
0 1 S67‑p DDCQDVAsECEVKCM
1 1 T76‑p CEVKCMPtFQFFkKG
0 4 K81‑ac MPtFQFFkKGQkVGE
0 1 K85‑sc QFFkKGQkVGEFSGA
0 6 K94‑ac GEFSGANkEkLEAtI
0 2 K94‑ub GEFSGANkEkLEAtI
0 1 K94‑sc GEFSGANkEkLEAtI
0 2 K96 FSGANkEKLEAtINE
0 12 K96‑ub FSGANkEkLEAtINE
1 1 T100‑p NkEkLEAtINELV__
  mouse

 
K3 _____MVKLIESkEA
K8‑ac MVKLIESkEAFQEAL
K8‑ub MVKLIESkEAFQEAL
K8‑sc MVKLIESkEAFQEAL
E9 VKLIESkEAFQEALA
K39‑ac CGPCKMIkPFFHsLC
K39‑ub CGPCKMIkPFFHsLC
K39 CGPCKMIKPFFHsLC
S44‑p MIkPFFHsLCDKYSN
C46 kPFFHsLCDKYSNVV
A67 DDCQDVAADCEVKCM
T76 CEVKCMPTFQFYkKG
K81‑ac MPTFQFYkKGQKVGE
K85 QFYkKGQKVGEFSGA
K94‑ac GEFSGANkEkLEASI
K94 GEFSGANKEkLEASI
K94 GEFSGANKEkLEASI
K96‑ac FSGANkEkLEASITE
K96‑ub FSGANkEkLEASITE
S100 NkEkLEASITEYA__
  rat

 
K3‑ac _____MVkLIESkEA
K8‑ac MVkLIESkEAFQEAL
K8 MVkLIESKEAFQEAL
K8 MVkLIESKEAFQEAL
E9 VkLIESkEAFQEALA
K39‑ac CGPCKMIkPFFHSLC
K39 CGPCKMIKPFFHSLC
K39 CGPCKMIKPFFHSLC
S44 MIkPFFHSLCDKYSN
C46 kPFFHSLCDKYSNVV
A67 DDCQDVAADCEVKCM
T76 CEVKCMPTFQFYKKG
K81 MPTFQFYKKGQKVGE
K85 QFYKKGQKVGEFSGA
K94‑ac GEFSGANkEkLEATI
K94 GEFSGANKEkLEATI
K94 GEFSGANKEkLEATI
K96‑ac FSGANkEkLEATITE
K96 FSGANkEKLEATITE
T100 NkEkLEATITEFA__
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