CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021861
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thioredoxin reductase 2, mitochondrial 
Protein Synonyms/Alias
 Thioredoxin reductase TR3 
Gene Name
 Txnrd2 
Gene Synonyms/Alias
 Trxr2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
153QLQDRKVKYFNIKASacetylation[1]
172HTVRGVDKGGKATLLacetylation[1]
285GCVPSHIKKLPTNQLacetylation[1]
329TRTLNLEKAGISTNPacetylation[1]
329TRTLNLEKAGISTNPubiquitination[2]
376PTAIKAGKLLAQRLFacetylation[1]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox- regulated cell signaling. 
Sequence Annotation
 NP_BIND 41 70 FAD (By similarity).
 ACT_SITE 497 497 Proton acceptor (By similarity).
 DISULFID 86 91 Redox-active (By similarity).
 CROSSLNK 522 523 Cysteinyl-selenocysteine (Cys-Sec) (By  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Redox-active center; Reference proteome; Selenocysteine; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 524 AA 
Protein Sequence
MVAAMVAALR GPSRRFRPRT RALTRGTRGA ASAAGGQQSF DLLVIGGGSG GLACAKEAAQ 60
LGKKVAVADY VEPSPRGTKW GLGGTCVNVG CIPKKLMHQA ALLGGMIRDA HHYGWEVAQP 120
VQHNWKTMAE AVQNHVKSLN WGHRVQLQDR KVKYFNIKAS FVDEHTVRGV DKGGKATLLS 180
AEHIVIATGG RPRYPTQVKG ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI 240
GLDTTVMMRS IPLRGFDQQM SSLVTEHMES HGTQFLKGCV PSHIKKLPTN QLQVTWEDHA 300
SGKEDTGTFD TVLWAIGRVP ETRTLNLEKA GISTNPKNQK IIVDAQEATS VPHIYAIGDV 360
AEGRPELTPT AIKAGKLLAQ RLFGKSSTLM DYSNVPTTVF TPLEYGCVGL SEEEAVALHG 420
QEHVEVYHAY YKPLEFTVAD RDASQCYIKM VCMREPPQLV LGLHFLGPNA GEVTQGFALG 480
IKCGASYAQV MQTVGIHPTC SEEVVKLHIS KRSGLEPTVT GCUG 524 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0004791; F:thioredoxin-disulfide reductase activity; ISS:UniProtKB.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0007507; P:heart development; IMP:MGI.
 GO:0030097; P:hemopoiesis; IMP:MGI.
 GO:0000305; P:response to oxygen radical; TAS:UniProtKB. 
Interpro
 IPR016156; FAD/NAD-linked_Rdtase_dimer.
 IPR013027; FAD_pyr_nucl-diS_OxRdtase.
 IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
 IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
 IPR012999; Pyr_OxRdtase_I_AS.
 IPR001327; Pyr_OxRdtase_NAD-bd_dom.
 IPR006338; Thioredoxin/glutathione_Rdtase. 
Pfam
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2
 PF02852; Pyr_redox_dim 
SMART
  
PROSITE
 PS00076; PYRIDINE_REDOX_1 
PRINTS
 PR00368; FADPNR.