CPLM-005827

Genbank Nucleotide ID

Peroxiredoxin-5, mitochondrial

Protein Synonyms/Alias

Alu corepressor 1; Antioxidant enzyme B166; AOEB166; Liver tissue 2D-page spot 71B; PLP; Peroxiredoxin V; Prx-V; Peroxisomal antioxidant enzyme; TPx type VI; Thioredoxin peroxidase PMP20; Thioredoxin reductase

Homo sapiens (Human)

Position	Peptide	Type	References
57	AAAMAPIKVGDAIPA	ubiquitination	[1]
75	FEGEPGNKVNLAELF	ubiquitination	[1]
83	VNLAELFKGKKGVLF	acetylation	[2, 3, 4, 5]
83	VNLAELFKGKKGVLF	ubiquitination	[1, 6, 7, 8]
86	AELFKGKKGVLFGVP	ubiquitination	[9, 10]
102	AFTPGCSKTHLPGFV	ubiquitination	[6, 9]
116	VEQAEALKAKGVQVV	acetylation	[2]

[1] 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]
[2] 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]
[3] 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]
[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] 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] 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]
[7] 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]
[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] 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]
[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]

Functional Description

Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.

DOMAIN 56 214 Thioredoxin.
MOTIF 212 214 Microbody targeting signal (By
ACT_SITE 100 100 Cysteine sulfenic acid (-SOH)
MOD_RES 83 83 N6-acetyllysine.
DISULFID 100 204 Redox-active.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO:0005829; C:cytosol; IDA:UniProtKB.
GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
GO:0005777; C:peroxisome; IDA:UniProtKB.
GO:0016209; F:antioxidant activity; IDA:UniProtKB.
GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
GO:0004601; F:peroxidase activity; IDA:UniProtKB.
GO:0051920; F:peroxiredoxin activity; IEA:EC.
GO:0072541; F:peroxynitrite reductase activity; IDA:UniProtKB.
GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO:0001016; F:RNA polymerase III regulatory region DNA binding; IDA:UniProtKB.
GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO:0070995; P:NADPH oxidation; IDA:UniProtKB.
GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO:0051354; P:negative regulation of oxidoreductase activity; IDA:UniProtKB.
GO:0016480; P:negative regulation of transcription from RNA polymerase III promoter; IDA:UniProtKB.
GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB.
GO:2001057; P:reactive nitrogen species metabolic process; IDA:UniProtKB.
GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; IDA:UniProtKB.

IPR013740; Redoxin.
IPR012336; Thioredoxin-like_fold.

PS51352; THIOREDOXIN_2