UniProt Accession

 PRDX1_HUMAN; Q06830; B5BU26; D3DPZ8; P35703; Q2V576; Q5T154; Q5T155 

Genbank Protein ID

 X67951; L19184; BT019740; CR407652; DQ297142; AB451262; AB451388; AL451136; AL451136; AL451136; CH471059; CH471059; CH471059; CH471059; CH471059; CH471059; CH471059; BC007063; BC021683 

Genbank Nucleotide ID

 CAA48137.1; AAA50464.1; AAV38545.1; CAG28580.1; ABB84465.1; BAG70076.1; BAG70202.1; CAI13095.1; CAI13096.1; CAI13097.1; EAX06975.1; EAX06976.1; EAX06978.1; EAX06979.1; EAX06980.1; EAX06981.1; EAX06982.1; AAH07063.1; AAH21683.1 

Protein Name

 Peroxiredoxin-1 

Protein Synonyms/Alias

 Natural killer cell-enhancing factor A; NKEF-A; Proliferation-associated gene protein; PAG; Thioredoxin peroxidase 2; Thioredoxin-dependent peroxide reductase 2 

Gene Name

 PRDX1 

Gene Synonyms/Alias

 PAGA; PAGB; TDPX2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
7	*MSSGNAKIGHPAPN	acetylation	[1, 2, 3, 4]
7	*MSSGNAKIGHPAPN	ubiquitination	[4, 5, 6, 7]
16	GHPAPNFKATAVMPD	acetylation	[1, 4]
16	GHPAPNFKATAVMPD	ubiquitination	[4, 6, 7, 8, 9, 10]
27	VMPDGQFKDISLSDY	acetylation	[1, 2, 3, 4, 11]
27	VMPDGQFKDISLSDY	ubiquitination	[4, 6, 7, 8, 10, 12, 13]
35	DISLSDYKGKYVVFF	acetylation	[1, 2, 3, 4]
35	DISLSDYKGKYVVFF	ubiquitination	[4, 8, 9, 10, 13, 14]
37	SLSDYKGKYVVFFFY	ubiquitination	[7]
67	SDRAEEFKKLNCQVI	ubiquitination	[8]
92	LAWVNTPKKQGGLGP	ubiquitination	[14]
93	AWVNTPKKQGGLGPM	ubiquitination	[4, 6, 7, 8, 10, 13, 14]
109	IPLVSDPKRTIAQDY	acetylation	[4, 15]
109	IPLVSDPKRTIAQDY	ubiquitination	[4, 6, 7, 8]
120	AQDYGVLKADEGISF	ubiquitination	[4, 7, 8, 9, 10, 14, 16]
136	GLFIIDDKGILRQIT	ubiquitination	[5, 6, 8, 9, 10, 12, 13]
168	QAFQFTDKHGEVCPA	acetylation	[3]
168	QAFQFTDKHGEVCPA	ubiquitination	[5, 14]
178	EVCPAGWKPGSDTIK	acetylation	[4]
178	EVCPAGWKPGSDTIK	ubiquitination	[5, 7, 9, 13, 14]
185	KPGSDTIKPDVQKSK	acetylation	[3, 4]
185	KPGSDTIKPDVQKSK	ubiquitination	[4, 7, 14]
192	KPDVQKSKEYFSKQK	ubiquitination	[6, 7]
197	KSKEYFSKQK*****	acetylation	[1, 2, 17]
197	KSKEYFSKQK*****	ubiquitination	[6, 7, 13]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [7] 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]
 [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] 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]
 [10] 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]
 [11] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [12] 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]
 [13] 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]
 [14] 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]
 [15] 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]
 [16] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [17] 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 but not 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). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). 

Sequence Annotation

 DOMAIN 6 165 Thioredoxin.
 ACT_SITE 52 52 Cysteine sulfenic acid (-SOH)
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 7 7 N6-acetyllysine.
 MOD_RES 16 16 N6-acetyllysine.
 MOD_RES 27 27 N6-acetyllysine.
 MOD_RES 35 35 N6-acetyllysine.
 MOD_RES 90 90 Phosphothreonine; by CDK1.
 DISULFID 52 52 Interchain (with C-173); in linked form.
 DISULFID 173 173 Interchain (with C-52); in linked form.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 199 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005759; C:mitochondrial matrix; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005719; C:nuclear euchromatin; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0005782; C:peroxisomal matrix; IEA:Compara.
 GO:0020037; F:heme binding; IEA:Compara.
 GO:0008379; F:thioredoxin peroxidase activity; IDA:BHF-UCL.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0034101; P:erythrocyte homeostasis; IEA:Compara.
 GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL.
 GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:Compara.
 GO:0042345; P:regulation of NF-kappaB import into nucleus; IEA:Compara.
 GO:0032872; P:regulation of stress-activated MAPK cascade; IEA:Compara.
 GO:0019430; P:removal of superoxide radicals; IEA:Compara.
 GO:0001501; P:skeletal system development; TAS:ProtInc. 

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