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Protein Page:
TXNRD2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
TXNRD2 Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox- regulated cell signaling. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Oxidoreductase; Nucleotide Metabolism - pyrimidine; EC 1.8.1.9
Cellular Component: mitochondrion; mitochondrial matrix
Molecular Function: protein binding; thioredoxin-disulfide reductase activity; FAD binding; NADP binding
Biological Process: response to oxygen radical; cell redox homeostasis; heart development; hemopoiesis
Reference #:  Q9NNW7 (UniProtKB)
Alt. Names/Synonyms: KIAA1652; Selenoprotein Z; SelZ; thioredoxin reductase 2; Thioredoxin reductase 2, mitochondrial; thioredoxin reductase 3; thioredoxin reductase beta; Thioredoxin reductase TR3; TR-beta; TR3; TRXR2; TXNRD2
Gene Symbols: TXNRD2
Molecular weight: 56,507 Da
Basal Isoelectric point: 7.24  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TXNRD2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: 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.


 MS 

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


       human

 
0 3 Y40-p AAAGQRDyDLLVVGG
0 2 R63 KEAAQLGRKVAVVDY
0 4 K137 EAVQNHVKSLNWGHR
0 14 K153-a QLQDRKVkYFNIKAS
0 1 K175-a CGVAKGGkEILLSAD
0 3 R285 GCAPSRVRRLPDGQL
0 1 K329 TRSLNLEKAGVDTSP
0 11 D337 AGVDTSPDTQKILVD
0 2 K432-a EVYHAHYkPLEFTVA
  mouse

 
F40 AAGGQQSFDLLVIGG
K63-a KEAAQLGkKVAVADY
K137-a EAVQNHVkSLNWGHR
K153 QLQDRKVKYFNIKAS
K175 RGVDKGGKATLLSAE
K285-a GCVPSHIkKLPTNQL
K329-u TRTLNLEkAGISTNP
K337-a AGISTNPkNQKIIVD
K432 EVYHAYYKPLEFTVA
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