CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-034230
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Thioredoxin reductase 2, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 Txnrd2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
63KEAAQLGKKVAVADYacetylation[1]
79EPSPRGTKWGLGGTCacetylation[2]
79EPSPRGTKWGLGGTCsuccinylation[2]
153QLQDRKVKYFNIKASacetylation[1]
158KVKYFNIKASFVDEHacetylation[2]
158KVKYFNIKASFVDEHsuccinylation[2]
175RGVDKGGKATLLSAEacetylation[2]
175RGVDKGGKATLLSAEsuccinylation[2]
285GCVPSHIKKLPTNQLacetylation[1]
329TRTLNLEKAGISTNPacetylation[2]
329TRTLNLEKAGISTNPsuccinylation[2]
329TRTLNLEKAGISTNPubiquitination[3]
337AGISTNPKNQKIIVDacetylation[2]
337AGISTNPKNQKIIVDsuccinylation[2]
Reference
 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; FAD; Flavoprotein; Oxidoreductase; Redox-active center; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 491 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 DYSNVYHAYY KPLEFTVADR DASQCYIKMV 420
CMREPPQLVL GLHFLGPNAG EVTQGFALGI KCGASYAQVM QTVGIHPTCS EEVVKLHISK 480
RSGLEPTVTG C 491 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0007507; P:heart development; IMP:MGI.
 GO:0030097; P:hemopoiesis; IMP:MGI. 
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.