CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006389
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxiredoxin TSA1 
Protein Synonyms/Alias
 Cytoplasmic thiol peroxidase 1; cTPx 1; PRP; Thiol-specific antioxidant protein 1; Thioredoxin peroxidase 
Gene Name
 TSA1 
Gene Synonyms/Alias
 TPX1; TSA; ZRG14; YML028W 
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
13QKQAPTFKKTAVVDGubiquitination[1]
14KQAPTFKKTAVVDGVubiquitination[1, 2]
29FDEVSLDKYKGKYVVacetylation[3]
29FDEVSLDKYKGKYVVubiquitination[2]
89AWTNIPRKEGGLGPIacetylation[4]
89AWTNIPRKEGGLGPIubiquitination[1, 2]
132GLFIIDPKGVIRHITacetylation[3]
132GLFIIDPKGVIRHITubiquitination[1, 2]
181TPGAATIKPTVEDSKubiquitination[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] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] 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]
 [4] Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures.
 Xie H, Bandhakavi S, Roe MR, Griffin TJ.
 J Proteome Res. 2007 May;6(5):2019-26. [PMID: 17397211
Functional Description
 Physiologically important antioxidant which constitutes an enzymatic defense against sulfur-containing radicals. Can provide protection against a thiol-containing oxidation system but not against an oxidation system without thiol. 
Sequence Annotation
 DOMAIN 3 161 Thioredoxin.
 ACT_SITE 48 48 Cysteine sulfenic acid (-SOH)
 MOD_RES 174 174 Phosphothreonine.
 DISULFID 48 48 Interchain (with C-171); in linked form
 DISULFID 48 48 Interchain (with C-84 in SRX1);
 DISULFID 171 171 Interchain (with C-48); in linked form  
Keyword
 3D-structure; Antioxidant; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 196 AA 
Protein Sequence
MVAQVQKQAP TFKKTAVVDG VFDEVSLDKY KGKYVVLAFI PLAFTFVCPT EIIAFSEAAK 60
KFEEQGAQVL FASTDSEYSL LAWTNIPRKE GGLGPINIPL LADTNHSLSR DYGVLIEEEG 120
VALRGLFIID PKGVIRHITI NDLPVGRNVD EALRLVEAFQ WTDKNGTVLP CNWTPGAATI 180
KPTVEDSKEY FEAANK 196 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005844; C:polysome; IDA:SGD.
 GO:0043022; F:ribosome binding; IDA:SGD.
 GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
 GO:0051082; F:unfolded protein binding; IMP:SGD.
 GO:0045454; P:cell redox homeostasis; IDA:SGD.
 GO:0034599; P:cellular response to oxidative stress; IDA:SGD.
 GO:0000077; P:DNA damage checkpoint; IGI:SGD.
 GO:0042262; P:DNA protection; IMP:SGD.
 GO:0006457; P:protein folding; IMP:SGD.
 GO:0001302; P:replicative cell aging; IMP:SGD.
 GO:0033194; P:response to hydroperoxide; IMP:SGD. 
Interpro
 IPR000866; AhpC/TSA.
 IPR024706; Peroxiredoxin_AhpC-typ.
 IPR019479; Peroxiredoxin_C.
 IPR012336; Thioredoxin-like_fold. 
Pfam
 PF10417; 1-cysPrx_C
 PF00578; AhpC-TSA 
SMART
  
PROSITE
 PS51352; THIOREDOXIN_2 
PRINTS