Peroxiredoxin 2

PRDX2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1QMV
Identifiers
Aliases	PRDX2, HEL-S-2a, NKEF-B, NKEFB, PRP, PRX2, PRXII, PTX1, TDPX1, TPX1, TSA, Peroxiredoxin 2
External IDs	OMIM: 600538 MGI: 109486 HomoloGene: 21182 GeneCards: PRDX2
Gene location (Human)
Chr.	Chromosome 19 (human)[1]
End	12,801,800 bp[1]
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)[2]
End	84,974,834 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• oxidoreductase activity; • antioxidant activity; • peroxiredoxin activity; • peroxidase activity; • GO:0001948 protein binding; • thioredoxin peroxidase activity;
Cellular component	• cytoplasm; • extracellular exosome; • cytosol;
Biological process	• regulation of apoptotic process; • negative regulation of apoptotic process; • oxidation-reduction process; • hydrogen peroxide catabolic process; • cell redox homeostasis; • response to oxidative stress; • cellular response to oxidative stress; • removal of superoxide radicals; • activation of MAPK activity; • respiratory burst involved in inflammatory response; • regulation of hydrogen peroxide metabolic process; • positive regulation of blood coagulation; • negative regulation of lipopolysaccharide-mediated signaling pathway; • negative regulation of NF-kappaB transcription factor activity; • response to lipopolysaccharide; • T cell proliferation; • hydrogen peroxide metabolic process; • negative regulation of T cell differentiation; • thymus development; • homeostasis of number of cells; • negative regulation of reactive oxygen species metabolic process; • negative regulation of extrinsic apoptotic signaling pathway; • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; • leukocyte activation;
	Sources:Amigo / QuickGO
Orthologs
	7001
	21672
	ENSG00000167815
	ENSMUSG00000005161
	P32119
	Q61171
	NM_181738; NM_005809; NM_181737
	NM_011563; NM_001317385
	NP_005800
	NP_001304314; NP_035693
	Wikidata
View/Edit Human	View/Edit Mouse

Peroxiredoxin-2 is a protein that in humans is encoded by the PRDX2 gene.[5][6]

This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. The crystal structure of this protein has been resolved to 0.27 nm (= 2.7 angstroms). Transcript variants encoding distinct isoforms have been identified for this gene.[6]

References

GRCh38: Ensembl release 89: ENSG00000167815 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000005161 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Pahl P, Berger R, Hart I, Chae HZ, Rhee SG, Patterson D (Aug 1995). "Localization of TDPX1, a human homologue of the yeast thioredoxin-dependent peroxide reductase gene (TPX), to chromosome 13q12". Genomics. 26 (3): 602–6. doi:10.1016/0888-7543(95)80183-M. PMID 7607688.
"Entrez Gene: PRDX2 peroxiredoxin 2".

Yao Y, Taylor M, Davey F, RenY, Aiton J , Coote P, Chen X, Yan SD & Gunn-Moore FJ. (2007). "Interaction of Amyloid binding Alcohol Dehydrogenase/Aβ mediates up-regulation of peroxiredoxin II in the brains of Alzheimer's disease patients and a transgenic Alzheimer's disease mouse model". Molecular and Cellular Neuroscience. 35 (2): 377–82. doi:10.1016/j.mcn.2007.03.013. PMID 17490890.CS1 maint: multiple names: authors list (link)
Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
Shau H, Butterfield LH, Chiu R, Kim A (1994). "Cloning and sequence analysis of candidate human natural killer-enhancing factor genes". Immunogenetics. 40 (2): 129–34. doi:10.1007/BF00188176. PMID 8026862.
Chae HZ, Robison K, Poole LB, et al. (1994). "Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes". Proc. Natl. Acad. Sci. U.S.A. 91 (15): 7017–21. doi:10.1073/pnas.91.15.7017. PMC 44329. PMID 8041738.
Lim YS, Cha MK, Yun CH, et al. (1994). "Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein". Biochem. Biophys. Res. Commun. 199 (1): 199–206. doi:10.1006/bbrc.1994.1214. PMID 8123012.
Lim YS, Cha MK, Kim HK, Kim IH (1994). "The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions". Gene. 140 (2): 279–84. doi:10.1016/0378-1119(94)90558-4. PMID 8144038.
Golaz O, Hughes GJ, Frutiger S, et al. (1994). "Plasma and red blood cell protein maps: update 1993". Electrophoresis. 14 (11): 1223–31. doi:10.1002/elps.11501401183. PMID 8313871.
Cha MK, Kim IH (1996). "Glutathione-linked thiol peroxidase activity of human serum albumin: a possible antioxidant role of serum albumin in blood plasma". Biochem. Biophys. Res. Commun. 222 (2): 619–25. doi:10.1006/bbrc.1996.0793. PMID 8670254.
Ji H, Reid GE, Moritz RL, et al. (1997). "A two-dimensional gel database of human colon carcinoma proteins". Electrophoresis. 18 (3–4): 605–13. doi:10.1002/elps.1150180344. PMID 9150948.
Wang ZM, Liu C, Dziarski R (2000). "Chemokines are the main proinflammatory mediators in human monocytes activated by Staphylococcus aureus, peptidoglycan, and endotoxin". J. Biol. Chem. 275 (27): 20260–7. doi:10.1074/jbc.M909168199. PMID 10751418.
Cha MK, Yun CH, Kim IH (2000). "Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane". Biochemistry. 39 (23): 6944–50. doi:10.1021/bi000034j. PMID 10841776.
Schröder E, Littlechild JA, Lebedev AA, et al. (2000). "Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution". Structure. 8 (6): 605–15. doi:10.1016/S0969-2126(00)00147-7. PMID 10873855.
Harris JR, Schröder E, Isupov MN, et al. (2001). "Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography". Biochim. Biophys. Acta. 1547 (2): 221–34. doi:10.1016/s0167-4838(01)00184-4. PMID 11410278.
Noh DY, Ahn SJ, Lee RA, et al. (2001). "Overexpression of peroxiredoxin in human breast cancer". Anticancer Res. 21 (3B): 2085–90. PMID 11497302.
Kim SH, Fountoulakis M, Cairns N, Lubec G (2002). "Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome". J. Neural Transm. Suppl. (61): 223–35. doi:10.1007/978-3-7091-6262-0_18. PMID 11771746.
Rabilloud T, Heller M, Gasnier F, et al. (2002). "Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site". J. Biol. Chem. 277 (22): 19396–401. doi:10.1074/jbc.M106585200. PMID 11904290.
Anahory T, Dechaud H, Bennes R, et al. (2002). "Identification of new proteins in follicular fluid of mature human follicles". Electrophoresis. 23 (7–8): 1197–202. doi:10.1002/1522-2683(200204)23:7/8<1197::AID-ELPS1197>3.0.CO;2-2. PMID 11981869.
Shen C, Nathan C (2002). "Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells". Mol. Med. 8 (2): 95–102. doi:10.1007/BF03402079. PMC 2039972. PMID 12080185.
Geiben-Lynn R, Kursar M, Brown NV, et al. (2003). "HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family". J. Biol. Chem. 278 (3): 1569–74. doi:10.1074/jbc.M209964200. PMID 12421812.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000167815 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000005161 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7607688-5] Pahl P, Berger R, Hart I, Chae HZ, Rhee SG, Patterson D (Aug 1995). "Localization of TDPX1, a human homologue of the yeast thioredoxin-dependent peroxide reductase gene (TPX), to chromosome 13q12". Genomics. 26 (3): 602–6. doi:10.1016/0888-7543(95)80183-M. PMID 7607688.

[entrez-6] "Entrez Gene: PRDX2 peroxiredoxin 2".

Oxidoreductases: peroxidases (EC 1.11)
1.11.1.1-14	NADH peroxidase NADPH peroxidase Fatty-acid peroxidase Catalase Cytochrome c peroxidase Eosinophil peroxidase Glutathione peroxidase GPX 1 2 3 4 5 6 7 8 Horseradish peroxidase Lactoperoxidase Myeloperoxidase Thyroid peroxidase Deiodinase Iodothyronine deiodinase Iodotyrosine deiodinase
1.11.1.15 (peroxiredoxin)	1 2 3 4 5 6

Peroxiredoxin 2

References

Further reading