CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030137
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thioredoxin reductase 1, cytoplasmic 
Protein Synonyms/Alias
 cDNA, FLJ92557, highly similar to Homo sapiens thioredoxin reductase 1 (TXNRD1), mRNA 
Gene Name
 TXNRD1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29SGGLAAAKEAAQYGKubiquitination[1, 2, 3, 4]
37EAAQYGKKVMVLDFVubiquitination[2, 5]
67VNVGCIPKKLMHQAAubiquitination[2, 5]
68NVGCIPKKLMHQAALubiquitination[2, 4, 6]
89DSRNYGWKVEETVKHubiquitination[1, 2, 3, 4, 7]
95WKVEETVKHDWDRMIubiquitination[2, 3, 4, 7]
124RVALREKKVVYENAYubiquitination[2, 3]
150TNNKGKEKIYSAERFubiquitination[2]
174YLGIPGDKEYCISSDubiquitination[1, 2]
235FDQDMANKIGEHMEEubiquitination[2, 4, 7]
246HMEEHGIKFIRQFVPubiquitination[1, 2, 3, 7]
255IRQFVPIKVEQIEAGubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
299GRDACTRKIGLETVGubiquitination[2, 3, 4, 5, 7]
308GLETVGVKINEKTGKubiquitination[1, 2, 3, 4, 7]
315KINEKTGKIPVTDEEubiquitination[2, 3, 7]
339IGDILEDKVELTPVAubiquitination[3]
364LYAGSTVKCDYENVPubiquitination[1, 2]
389ACGLSEEKAVEKFGEubiquitination[1, 2]
424DNNKCYAKIICNTKDubiquitination[1, 2]
430AKIICNTKDNERVVGubiquitination[2, 4, 7]
457QGFAAALKCGLTKKQubiquitination[1, 2, 4, 5]
463LKCGLTKKQLDSTIGubiquitination[2]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] 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]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] 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]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; FAD; Flavoprotein; Oxidoreductase; Redox-active center; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 497 AA 
Protein Sequence
MNGPEDLPKS YDYDLIIIGG GSGGLAAAKE AAQYGKKVMV LDFVTPTPLG TRWGLGGTCV 60
NVGCIPKKLM HQAALLGQAL QDSRNYGWKV EETVKHDWDR MIEAVQNHIG SLNWGYRVAL 120
REKKVVYENA YGQFIGPHRI KATNNKGKEK IYSAERFLIA TGERPRYLGI PGDKEYCISS 180
DDLFSLPYCP GKTLVVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM 240
EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVMLA IGRDACTRKI 300
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEDKV ELTPVAIQAG RLLAQRLYAG 360
STVKCDYENV PTTVFTPLEY GACGLSEEKA VEKFGEENIE VYHSYFWPLE WTIPSRDNNK 420
CYAKIICNTK DNERVVGFHV LGPNAGEVTQ GFAAALKCGL TKKQLDSTIG IHPVCAEVFT 480
TLSVTKRSGA SILQAGC 497 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0045340; F:mercury ion binding; IEA:Compara.
 GO:0016174; F:NAD(P)H oxidase activity; IEA:Compara.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0033797; F:selenate reductase activity; IEA:Compara.
 GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:Compara.
 GO:0042537; P:benzene-containing compound metabolic process; IEA:Compara.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0071280; P:cellular response to copper ion; IEA:Compara.
 GO:0071455; P:cellular response to hyperoxia; IEA:Compara.
 GO:0006749; P:glutathione metabolic process; IEA:Compara.
 GO:0070276; P:halogen metabolic process; IEA:Compara.
 GO:0042744; P:hydrogen peroxide catabolic process; IEA:Compara.
 GO:0001707; P:mesoderm formation; IEA:Compara.
 GO:0042191; P:methylmercury metabolic process; IEA:Compara.
 GO:0070995; P:NADPH oxidation; IEA:Compara.
 GO:0001890; P:placenta development; IEA:Compara.
 GO:0010942; P:positive regulation of cell death; IEA:Compara.
 GO:0051262; P:protein tetramerization; IEA:Compara.
 GO:0048678; P:response to axon injury; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0010269; P:response to selenium ion; IEA:Compara.
 GO:0016259; P:selenocysteine metabolic process; IEA:Compara. 
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.