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Protein Page:
TXNRD2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Nucleotide Metabolism - pyrimidine; Oxidoreductase; 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 4 Y40-p AAAGQRDyDLLVVGG
0 2 R63 KEAAQLGRKVAVVDY
0 1 K94-ub VNVGCIPkKLMHQAA
0 5 K137-ac EAVQNHVkSLNWGHR
0 14 K153-ac QLQDRKVkYFNIKAS
0 1 K175-ac CGVAKGGkEILLSAD
0 1 K215 SDDIFWLKESPGKTL
0 1 K215 SDDIFWLKESPGKTL
0 1 T238-p LECAGFLtGIGLDtt
0 1 T244-p LtGIGLDttIMMRsI
0 1 T245-p tGIGLDttIMMRsIP
0 1 S250-p DttIMMRsIPLRGFD
0 3 R285 GCAPSRVRRLPDGQL
0 1 K329 TRSLNLEKAGVDTSP
0 1 K329 TRSLNLEKAGVDTSP
0 1 K329 TRSLNLEKAGVDTSP
0 11 D337 AGVDTSPDTQKILVD
0 1 D337 AGVDTSPDTQKILVD
0 2 K432-ac EVYHAHYkPLEFTVA
0 1 K506-ac TCSEEVVkLRISKRS
  mouse

 
F40 AAGGQQSFDLLVIGG
K63-ac KEAAQLGkKVAVADY
K94 VNVGCIPKKLMHQAA
K137-ac EAVQNHVkSLNWGHR
K153 QLQDRKVKYFNIKAS
K175 RGVDKGGKATLLSAE
K215-ac SDDIFWLkESPGKTL
K215-sc SDDIFWLkESPGKTL
T238 LECAGFLTGIGLDTT
T244 LTGIGLDTTVMMRSI
T245 TGIGLDTTVMMRSIP
S250 DTTVMMRSIPLRGFD
K285-ac GCVPSHIkKLPTNQL
K329-ac TRTLNLEkAGISTNP
K329-ub TRTLNLEkAGISTNP
K329-sc TRTLNLEkAGISTNP
K337-ac AGISTNPkNQKIIVD
K337-sc AGISTNPkNQKIIVD
K432 EVYHAYYKPLEFTVA
K506 TCSEEVVKLHISKRS
  rat

 
F42 AAGGQQNFDLLVIGG
R65 KEAAQLGRKVAVADY
K96 VNVGCIPKKLMHQAA
K139 EAVQNHVKSLNWGHR
K155 QLQDRKVKYFNIKAS
K177 HGVDKAGKVTQLSAK
K217 SDDIFWLKESPGKTL
K217 SDDIFWLKESPGKTL
T240 LECAGFLTGIGLDTT
T246 LTGIGLDTTVMMRSV
T247 TGIGLDTTVMMRSVP
S252 DTTVMMRSVPLRGFD
R287 GCVPSLIRKLPTNQL
K331 TRNLNLEKAGVNTNP
K331 TRNLNLEKAGVNTNP
K331 TRNLNLEKAGVNTNP
K339 AGVNTNPKNQKIIVD
K339 AGVNTNPKNQKIIVD
K434 EVYHAYYKPLEFTVA
K508 TCSEEVVKLHISKRS
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