CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021929
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thioredoxin reductase 2, mitochondrial 
Protein Synonyms/Alias
 Selenoprotein Z; SelZ; TR-beta; Thioredoxin reductase TR3 
Gene Name
 TXNRD2 
Gene Synonyms/Alias
 KIAA1652; TRXR2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
153QLQDRKVKYFNIKASacetylation[1]
175CGVAKGGKEILLSADacetylation[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
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; Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Polymorphism; Redox-active center; Reference proteome; Selenocysteine; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 524 AA 
Protein Sequence
MAAMAVALRG LGGRFRWRTQ AVAGGVRGAA RGAAAGQRDY DLLVVGGGSG GLACAKEAAQ 60
LGRKVAVVDY VEPSPQGTRW GLGGTCVNVG CIPKKLMHQA ALLGGLIQDA PNYGWEVAQP 120
VPHDWRKMAE AVQNHVKSLN WGHRVQLQDR KVKYFNIKAS FVDEHTVCGV AKGGKEILLS 180
ADHIIIATGG RPRYPTHIEG ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI 240
GLDTTIMMRS IPLRGFDQQM SSMVIEHMAS HGTRFLRGCA PSRVRRLPDG QLQVTWEDST 300
TGKEDTGTFD TVLWAIGRVP DTRSLNLEKA GVDTSPDTQK ILVDSREATS VPHIYAIGDV 360
VEGRPELTPI AIMAGRLLVQ RLFGGSSDLM DYDNVPTTVF TPLEYGCVGL SEEEAVARHG 420
QEHVEVYHAH YKPLEFTVAG RDASQCYVKM VCLREPPQLV LGLHFLGPNA GEVTQGFALG 480
IKCGASYAQV MRTVGIHPTC SEEVVKLRIS KRSGLDPTVT 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; IEA:Compara.
 GO:0030097; P:hemopoiesis; IEA:Compara.
 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.