fbpx
Wikipedia

Peroxiredoxin 2

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

PRDX2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPRDX2, HEL-S-2a, NKEF-B, NKEFB, PRP, PRX2, PRXII, PTX1, TDPX1, TPX1, TSA, Peroxiredoxin 2
External IDsOMIM: 600538 MGI: 109486 HomoloGene: 21182 GeneCards: PRDX2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_181738
NM_005809
NM_181737

NM_011563
NM_001317385

RefSeq (protein)

NP_005800

NP_001304314
NP_035693

Location (UCSC)Chr 19: 12.8 – 12.8 MbChr 8: 85.7 – 85.7 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

PRDX2 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 edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167815 – Ensembl, May 2017
  2. ^ a b c 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.
  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.
  6. ^ a b "Entrez Gene: PRDX2 peroxiredoxin 2".

Further reading edit

  • 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. S2CID 2415008.{{cite journal}}: 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. S2CID 41855774.
  • 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. S2CID 7778993.
  • 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. Bibcode:1994PNAS...91.7017C. 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. S2CID 21447827.
  • 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. S2CID 25454450.
  • 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". Protein Expression in Down Syndrome Brain. pp. 223–35. doi:10.1007/978-3-7091-6262-0_18. ISBN 978-3-211-83704-7. PMID 11771746. {{cite book}}: |journal= ignored (help)
  • 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. S2CID 24574562.
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

peroxiredoxin, peroxiredoxin, protein, that, humans, encoded, prdx2, gene, prdx2available, structurespdbortholog, search, pdbe, rcsblist, codes1qmvidentifiersaliasesprdx2, nkef, nkefb, prx2, prxii, ptx1, tdpx1, tpx1, external, idsomim, 600538, 109486, homologe. Peroxiredoxin 2 is a protein that in humans is encoded by the PRDX2 gene 5 6 PRDX2Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1QMVIdentifiersAliasesPRDX2 HEL S 2a NKEF B NKEFB PRP PRX2 PRXII PTX1 TDPX1 TPX1 TSA Peroxiredoxin 2External IDsOMIM 600538 MGI 109486 HomoloGene 21182 GeneCards PRDX2Gene location Human Chr Chromosome 19 human 1 Band19p13 13Start12 796 820 bp 1 End12 801 800 bp 1 Gene location Mouse Chr Chromosome 8 mouse 2 Band8 C3 8 41 4 cMStart85 696 216 bp 2 End85 701 463 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed intrabecular boneexternal globus pallidusponsright ventricleleft adrenal glandsuperior vestibular nucleusembryoprefrontal cortexleft ventricleganglionic eminenceTop expressed insuperior frontal gyruslipyolk sacmotor neuronmaxillary prominenceaortic valvesecondary oocyteneural tubeascending aortatrigeminal ganglionMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionoxidoreductase activity antioxidant activity peroxiredoxin activity peroxidase activity protein binding thioredoxin peroxidase activityCellular componentcytoplasm extracellular exosome cytosolBiological processregulation of apoptotic process negative regulation of apoptotic process hydrogen peroxide catabolic process cell redox homeostasis response to oxidative stress cellular response to oxidative stress removal of superoxide radicals 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 activationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez700121672EnsemblENSG00000167815ENSMUSG00000005161UniProtP32119Q61171RefSeq mRNA NM 181738NM 005809NM 181737NM 011563NM 001317385RefSeq protein NP 005800NP 001304314NP 035693Location UCSC Chr 19 12 8 12 8 MbChr 8 85 7 85 7 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse PRDX2 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 edit a b c GRCh38 Ensembl release 89 ENSG00000167815 Ensembl May 2017 a b c 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 a b Entrez Gene PRDX2 peroxiredoxin 2 Further reading editYao Y Taylor M Davey F RenY Aiton J Coote P Chen X Yan SD amp Gunn Moore FJ 2007 Interaction of Amyloid binding Alcohol Dehydrogenase Ab 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 S2CID 2415008 a href Template Cite journal html title Template Cite journal cite journal a 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 S2CID 41855774 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 S2CID 7778993 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 Bibcode 1994PNAS 91 7017C 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 S2CID 21447827 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 S2CID 25454450 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 Schroder 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 Schroder 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 Protein Expression in Down Syndrome Brain pp 223 35 doi 10 1007 978 3 7091 6262 0 18 ISBN 978 3 211 83704 7 PMID 11771746 a href Template Cite book html title Template Cite book cite book a journal ignored help 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 lt 1197 AID ELPS1197 gt 3 0 CO 2 2 PMID 11981869 S2CID 24574562 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 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 nbsp This article on a gene on human chromosome 19 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Peroxiredoxin 2 amp oldid 1191467182, wikipedia, wiki, book, books, library,

article

, read, download, free, free download, mp3, video, mp4, 3gp, jpg, jpeg, gif, png, picture, music, song, movie, book, game, games.