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Showing Protein Peroxiredoxin-2 (HMDBP03017)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP03017
Secondary Accession Numbers
  • 8542
Name Peroxiredoxin-2
Synonyms
  1. NKEF-B
  2. Natural killer cell-enhancing factor B
  3. PRP
  4. TSA
  5. Thiol-specific antioxidant protein
  6. Thioredoxin peroxidase 1
  7. Thioredoxin-dependent peroxide reductase 1
Gene Name PRDX2
Protein Type Unknown
Biological Properties
General Function Involved in antioxidant activity
Specific Function 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).
Pathways Not Available
Reactions
R'-SH + ROOH → R'-S-S-R' + Water + ROH details
GO Classification
Biological Process
negative regulation of apoptotic process
removal of superoxide radicals
hydrogen peroxide catabolic process
Cellular Component
cytoplasm
Function
peroxiredoxin activity
catalytic activity
antioxidant activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity
Molecular Function
thioredoxin peroxidase activity
Process
cellular process
cellular homeostasis
cell redox homeostasis
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 19
Locus 19p13.2
SNPs PRDX2
Gene Sequence 
>597 bp
ATGGCCTCCGGTAACGCGCGCATCGGAAAGCCAGCCCCTGACTTCAAGGCCACAGCGGTG
GTTGATGGCGCCTTCAAAGAGGTGAAGCTGTCGGACTACAAAGGGAAGTACGTGGTCCTC
TTTTTCTACCCTCTGGACTTCACTTTTGTGTGCCCCACCGAGATCATCGCGTTCACAACC
GTGAAGAGGACTTCCGCAAAGCTGGGCTGTGAAGTGCTGGGCGTCTCGGTGGACTCTCAG
TTCACCCACCTGGCTTGGATCAACACCCCCCGGAAAGAGGGAGGCTTGGGCCCCTTGAAC
ATCCCCCTGCTTGCTGACGTGACCAGACGCTTGTCTGAGGATTACGGCGTGCTGAAAAAC
GATGAGGGCATTGCTTACAGGGGCCTCTTTATCATCGATGGCAAGGGTGTCCTTCGCCAG
ATCACTGTTAATGATTTGCCTGTGGGACGCTCCGTGGATGAGGCTCTGCGGCTGGTCCAG
GCCTTCCAGTACACAGACGAGCATGGGGAAGTTTGTCCGGCTGCTTGGAAGCCTGGACGT
GACACGATTAAGCCGAACGTGGATGACAGCAAGGAATATTTCTCCAAACACAATTAG
Protein Properties
Number of Residues 198
Molecular Weight 21891.725
Theoretical pI 5.972
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Peroxiredoxin-2
MASGNARIGKPAPDFKATAVVDGAFKEVKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSN
RAEDFRKLGCEVLGVSVDSQFTHLAWINTPRKEGGLGPLNIPLLADVTRRLSEDYGVLKT
DEGIAYRGLFIIDGKGVLRQITVNDLPVGRSVDEALRLVQAFQYTDEHGEVCPAGWKPGS
DTIKPNVDDSKEYFSKHN
GenBank ID Protein 438069
UniProtKB/Swiss-Prot ID P32119
UniProtKB/Swiss-Prot Entry Name PRDX2_HUMAN
PDB IDs
GenBank Gene ID Z22548
GeneCard ID PRDX2
GenAtlas ID PRDX2
HGNC ID HGNC:9353
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  3. Golaz O, Hughes GJ, Frutiger S, Paquet N, Bairoch A, Pasquali C, Sanchez JC, Tissot JD, Appel RD, Walzer C, et al.: Plasma and red blood cell protein maps: update 1993. Electrophoresis. 1993 Nov;14(11):1223-31. [PubMed:8313871 ]
  4. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed:1286667 ]
  5. Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed:9150948 ]
  6. Shau H, Butterfield LH, Chiu R, Kim A: Cloning and sequence analysis of candidate human natural killer-enhancing factor genes. Immunogenetics. 1994;40(2):129-34. [PubMed:8026862 ]
  7. Chevallet M, Wagner E, Luche S, van Dorsselaer A, Leize-Wagner E, Rabilloud T: Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress. J Biol Chem. 2003 Sep 26;278(39):37146-53. Epub 2003 Jul 8. [PubMed:12853451 ]
  8. Lim YS, Cha MK, Kim HK, Kim IH: The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions. Gene. 1994 Mar 25;140(2):279-84. [PubMed:8144038 ]
  9. Cha MK, Kim IH: Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell. Biochem Biophys Res Commun. 1995 Dec 26;217(3):900-7. [PubMed:8554614 ]
  10. Rabilloud T, Heller M, Gasnier F, Luche S, Rey C, Aebersold R, Benahmed M, Louisot P, Lunardi J: Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site. J Biol Chem. 2002 May 31;277(22):19396-401. Epub 2002 Mar 19. [PubMed:11904290 ]
  11. Gotter AL, Suppa C, Emanuel BS: Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors. J Mol Biol. 2007 Feb 9;366(1):36-52. Epub 2006 Nov 3. [PubMed:17141802 ]
  12. Schroder E, Littlechild JA, Lebedev AA, Errington N, Vagin AA, Isupov MN: Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution. Structure. 2000 Jun 15;8(6):605-15. [PubMed:10873855 ]