CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005792
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thioredoxin reductase 1 
Protein Synonyms/Alias
  
Gene Name
 TRR1 
Gene Synonyms/Alias
 YDR353W; D9476.5 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
77RMREQSTKFGTEIITubiquitination[1]
95SKVDLSSKPFKLWTEacetylation[2]
179FLTKYGSKVFMLVRKubiquitination[1]
221LEAKGDGKLLNALRIacetylation[2]
293AGDVQDSKYRQAITSacetylation[2]
293AGDVQDSKYRQAITSubiquitination[1]
313MAALDAEKYLTSLE*ubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Acts on thioredoxins 1 and 2. 
Sequence Annotation
 NP_BIND 11 14 FAD.
 NP_BIND 40 41 FAD.
 NP_BIND 295 297 FAD.
 BINDING 45 45 FAD; via amide nitrogen.
 BINDING 54 54 FAD.
 BINDING 87 87 FAD; via amide nitrogen and carbonyl
 BINDING 145 145 FAD.
 BINDING 288 288 FAD.
 MOD_RES 303 303 Phosphoserine.
 DISULFID 142 145 Redox-active.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase; Phosphoprotein; Redox-active center; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 319 AA 
Protein Sequence
MVHNKVTIIG SGPAAHTAAI YLARAEIKPI LYEGMMANGI AAGGQLTTTT EIENFPGFPD 60
GLTGSELMDR MREQSTKFGT EIITETVSKV DLSSKPFKLW TEFNEDAEPV TTDAIILATG 120
ASAKRMHLPG EETYWQKGIS ACAVCDGAVP IFRNKPLAVI GGGDSACEEA QFLTKYGSKV 180
FMLVRKDHLR ASTIMQKRAE KNEKIEILYN TVALEAKGDG KLLNALRIKN TKKNEETDLP 240
VSGLFYAIGH TPATKIVAGQ VDTDEAGYIK TVPGSSLTSV PGFFAAGDVQ DSKYRQAITS 300
AGSGCMAALD AEKYLTSLE 319 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
 GO:0008198; F:ferrous iron binding; IDA:SGD.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:SGD.
 GO:0045454; P:cell redox homeostasis; IDA:SGD.
 GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
 GO:0019430; P:removal of superoxide radicals; IEA:InterPro. 
Interpro
 IPR013027; FAD_pyr_nucl-diS_OxRdtase.
 IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
 IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
 IPR001327; Pyr_OxRdtase_NAD-bd_dom.
 IPR000103; Pyridine_nuc-diS_OxRdtase_2.
 IPR005982; Thioredox_Rdtase. 
Pfam
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2 
SMART
  
PROSITE
 PS00573; PYRIDINE_REDOX_2 
PRINTS
 PR00368; FADPNR.
 PR00469; PNDRDTASEII.