UniProt Accession

 PRDX2_HUMAN; P32119; A8K0C0; P31945; P32118; P35701; Q6FHG4; Q92763; Q9UC23 

Genbank Protein ID

 Z22548; L19185; CR450356; CR541789; AK289485; DQ231563; AC018761; CH471106; BC000452; BC003022; BC039428; X82321 

Genbank Nucleotide ID

 CAA80269.1; AAA50465.1; CAG29352.1; CAG46588.1; BAF82174.1; ABB02182.1; EAW84311.1; AAH00452.1; AAH03022.1; AAH39428.1; CAA57764.1 

Protein Name

 Peroxiredoxin-2 

Protein Synonyms/Alias

 Natural killer cell-enhancing factor B; NKEF-B; PRP; Thiol-specific antioxidant protein; TSA; Thioredoxin peroxidase 1; Thioredoxin-dependent peroxide reductase 1 

Gene Name

 PRDX2 

Gene Synonyms/Alias

 NKEFB; TDPX1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
10	SGNARIGKPAPDFKA	ubiquitination	[1, 2]
16	GKPAPDFKATAVVDG	ubiquitination	[2, 3]
26	AVVDGAFKEVKLSDY	ubiquitination	[3, 4]
92	AWINTPRKEGGLGPL	ubiquitination	[1, 3]
119	SEDYGVLKTDEGIAY	acetylation	[5]
119	SEDYGVLKTDEGIAY	ubiquitination	[1, 2, 3, 4, 6, 7, 8, 9]
135	GLFIIDGKGVLRQIT	ubiquitination	[1, 3, 7, 8, 9, 10]
191	KPNVDDSKEYFSKHN	ubiquitination	[1, 9]
196	DSKEYFSKHN*****	acetylation	[11]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [11] HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation.
 Parmigiani RB, Xu WS, Venta-Perez G, Erdjument-Bromage H, Yaneva M, Tempst P, Marks PA.
 Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9633-8. [PMID: 18606987] 

Functional Description

 Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). 

Sequence Annotation

 DOMAIN 6 164 Thioredoxin.
 ACT_SITE 51 51 Cysteine sulfenic acid (-SOH)
 MOD_RES 2 2 N-acetylalanine.
 DISULFID 51 51 Interchain (with C-172); in linked form
 DISULFID 172 172 Interchain (with C-51); in linked form  

Keyword

 3D-structure; Acetylation; Alternative splicing; Antioxidant; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase; Polymorphism; Redox-active center; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 198 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0008379; F:thioredoxin peroxidase activity; IDA:UniProtKB.
 GO:0042744; P:hydrogen peroxide catabolic process; TAS:BHF-UCL.
 GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0019430; P:removal of superoxide radicals; IDA:BHF-UCL. 

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