CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005824
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxiredoxin-6 
Protein Synonyms/Alias
 1-Cys peroxiredoxin; 1-Cys PRX; 24 kDa protein; Acidic calcium-independent phospholipase A2; aiPLA2; Antioxidant protein 2; Liver 2D page spot 40; Non-selenium glutathione peroxidase; NSGPx; Red blood cells page spot 12 
Gene Name
 PRDX6 
Gene Synonyms/Alias
 AOP2; KIAA0106 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
56TELGRAAKLAPEFAKubiquitination[1, 2]
63KLAPEFAKRNVKLIAacetylation[3, 4]
63KLAPEFAKRNVKLIAubiquitination[1, 5, 6]
97NCEEPTEKLPFPIIDubiquitination[1, 7]
125DPAEKDEKGMPVTARubiquitination[8]
182VATPVDWKDGDSVMVubiquitination[1, 7, 8]
199TIPEEEAKKLFPKGVubiquitination[8]
204EAKKLFPKGVFTKELubiquitination[1]
209FPKGVFTKELPSGKKacetylation[3, 4, 9, 10]
209FPKGVFTKELPSGKKubiquitination[1, 5, 6, 11, 12]
215TKELPSGKKYLRYTPacetylation[13]
216KELPSGKKYLRYTPQacetylation[13]
Reference
 [1] 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]
 [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] 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]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] 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]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] 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]
 [8] 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]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] 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]
 [11] 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]
 [12] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [13] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330
Functional Description
 Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. 
Sequence Annotation
 DOMAIN 5 169 Thioredoxin.
 ACT_SITE 32 32 For phospholipase activity.
 ACT_SITE 47 47 Cysteine sulfenic acid (-SOH)
 MOD_RES 44 44 Phosphothreonine.
 MOD_RES 63 63 N6-acetyllysine.
 MOD_RES 89 89 Phosphotyrosine.
 MOD_RES 209 209 N6-acetyllysine.
 DISULFID 47 47 Interchain; in linked form (By  
Keyword
 3D-structure; Acetylation; Antioxidant; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism; Lysosome; Multifunctional enzyme; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 224 AA 
Protein Sequence
MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE 60
FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF PIIDDRNREL AILLGMLDPA 120
EKDEKGMPVT ARVVFVFGPD KKLKLSILYP ATTGRNFDEI LRVVISLQLT AEKRVATPVD 180
WKDGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP 224 
Gene Ontology
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; NAS:UniProtKB.
 GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
 GO:0016209; F:antioxidant activity; NAS:UniProtKB.
 GO:0004602; F:glutathione peroxidase activity; IEA:EC.
 GO:0051920; F:peroxiredoxin activity; IEA:EC.
 GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
 GO:0042744; P:hydrogen peroxide catabolic process; IEA:Compara.
 GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
 GO:0006979; P:response to oxidative stress; IDA:UniProtKB. 
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