CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-042695
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Thioredoxin reductase 3 
Protein Synonyms/Alias
  
Gene Name
 TXNRD3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
155LSEITNQKTVPNIFVubiquitination[1, 2, 3]
266QALCDSRKFGWEYNQubiquitination[2]
442VMVQQLEKGSPGKLKubiquitination[2]
489GLEKIGVKINEKSGKubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; FAD; Flavoprotein; Oxidoreductase; Redox-active center; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 644 AA 
Protein Sequence
VASEGSVRRP SGPVPAPQPP AFRFVSRPGR ARSESETLER SPPQSPGPGK AGDAPNRRSG 60
HVRGARVLSP PGRRARLSSP GPSRSSEARE ELRRHLVGLI ERSRVVIFSK SYCPHSTRVK 120
ELFSSLGVEC NVLELDQVDD GARVQEVLSE ITNQKTVPNI FVNKVHVGGC DQTFQAYQSG 180
LLQKLLQEDL AYDYDLIIIG GGSGGLSCAK EAAILGKKVM VLDFVVPSPQ GTSWGLGGTC 240
VNVGCIPKKL MHQAALLGQA LCDSRKFGWE YNQQVRHNWE TMTKAIQNHI SSLNWGYRLS 300
LREKAVAYVN SYGEFVEHHK IKATNKKGQE TYYTAAQFVI ATGERPRYLG IQGDKEYCIT 360
SDDLFSLPYC PGKTLVVGAS YVALECAGFL AGFGLDVTVM VRSILLRGFD QEMAEKVGSY 420
MEQHGVKFLR KFIPVMVQQL EKGSPGKLKV LAKSTEGTET IEGVYNTVLL AIGRDSCTRK 480
IGLEKIGVKI NEKSGKIPVN DVEQTNVPYV YAVGDILEDK PELTPVAIQS GKLLAQRLFG 540
ASLEKIYHTL FWPLEWTVAG RENNTCYAKI ICNKFDHDRV IGFHILGPNA GEVTQGFAAA 600
MKCGLTKQLL DDTIGIHPTC GEVFTTLEIT KSSGLDITQK GCCG 644 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro. 
Interpro
 IPR016156; FAD/NAD-linked_Rdtase_dimer.
 IPR013027; FAD_pyr_nucl-diS_OxRdtase.
 IPR002109; Glutaredoxin.
 IPR011899; Glutaredoxin_euk/vir.
 IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
 IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
 IPR012999; Pyr_OxRdtase_I_AS.
 IPR001327; Pyr_OxRdtase_NAD-bd_dom.
 IPR012336; Thioredoxin-like_fold.
 IPR006338; Thioredoxin/glutathione_Rdtase. 
Pfam
 PF00462; Glutaredoxin
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2
 PF02852; Pyr_redox_dim 
SMART
  
PROSITE
 PS51354; GLUTAREDOXIN_2
 PS00076; PYRIDINE_REDOX_1 
PRINTS
 PR00368; FADPNR.