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FLASH GENE
Symbol PRDX2 contributors: np/shn - updated : 03-09-2014
HGNC name peroxiredoxin 2
HGNC id 9353
Location 19p13.2      Physical location : 12.907.634 - 12.912.694
Synonym name
  • thioredoxin-dependent peroxide reductase 1
  • thioredoxin peroxidase 1
  • natural killer-enhancing factor B
  • thiol-specific antioxidant 1
  • torin
  • Synonym symbol(s) TDPX1, PRP, TSA, NKEFB, PDX2, PRXII, PRX2, MGC4104
    EC.number 1.11.1.15
    DNA
    TYPE functioning gene
    STRUCTURE 5.06 kb     6 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    MAPPING cloned Y linked N status confirmed
    Map pter - D19S906 - D19S221 - PRDX2 - D19S914 - D19S840 - cen
    Physical map
    ZNF442 19p13.13 zinc finger protein 442 LOC388510 19 LOC388510 LOC90576 19p13.2 hypothetical protein LOC90576 ZNF443 19p13.13 zinc finger protein 443 FLJ38281 19p13.2 hypothetical protein FLJ38281 MGC26914 19p13.2 hypothetical protein MGC26914 PGK1P2 6p21-p12 phosphoglycerate kinase 1, pseudogene 2 ZNF490 19p13.2 zinc finger protein 490 FLJ90396 19p13.2 hypothetical protein FLJ90396 MGC4238 19p13.2 hypothetical protein MGC4238 LOC284393 19p13.2 similar to 60S ribosomal protein L10 (QM protein homolog) MAN2B1 19p13.2-p13.1 mannosidase, alpha, class 2B, member 1 PTD008 19p13.2 PTD008 protein DHPS 19p13.12-p13.11 deoxyhypusine synthase MGC10870 19p13.2 hypothetical protein MGC10870 TNPO2 19p13.2 transportin 2 (importin 3, karyopherin beta 2b) MGC2803 19p13.2 hypothetical protein MGC2803 ASNA1 19q13.3 arsA arsenite transporter, ATP-binding, homolog 1 (bacterial) VMD2L1 19p13.2-p13.12 arsA arsenite transporter, ATP-binding, homolog 1 (bacterial) HOOK2 19p13.2 arsA arsenite transporter, ATP-binding, homolog 1 (bacterial) RNASEH2A 19p13.2 ribonuclease H2, large subunit JUNB 19p13.2 jun B proto-oncogene PRDX2 13q12 peroxiredoxin 2 RTBDN 19p12 retbindin DNASE2 19p13.2 deoxyribonuclease II, lysosomal KLF1 19p13.13-p13.12 Kruppel-like factor 1 (erythroid) GCDH 19p13.2 glutaryl-Coenzyme A dehydrogenase FARSLA 19p13.2 phenylalanine-tRNA synthetase-like, alpha subunit CALR 19p13.3-p13.2 calreticulin RAD23A 19p13.2 RAD23 homolog A (S. cerevisiae) PLINP-1 19p13.2 papillomavirus L2 interacting nuclear protein 1 FLJ38607 19p13.2 hypothetical protein FLJ38607 LOC339375 19p13.13 hypothetical LOC339375 NFIX 19p13.2 nuclear factor I/X (CCAAT-binding transcription factor) LYL1 19p13.2-p13.1 lymphoblastic leukemia derived sequence 1 FLJ20244 19p13.13 hypothetical protein FLJ20244 BTBD14B 19p13.13 BTB (POZ) domain containing 14B
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    6 splicing 1039 21.8 198 - 1995 7607688
    3 splicing 710 15.8 142 - 1995 7607688
  • using an alternative splice site compared to variant 1, which results in a translational frameshift
  • EXPRESSION
    Type
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Visualeyeanterior segmentiris   Homo sapiens
     eyeretina    Homo sapiens
     eyesclera    Homo sapiens
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Nervouscentral    Homo sapiensFetal
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Blood/Hematopoieticerythrocyte Homo sapiens
    Nervousglia Homo sapiens
    Nervousneuron Homo sapiens
    Visualcone photoreceptor Homo sapiens
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • N-terminal domain of PRDX2 is necessary for its binding to Hb
  • mono polymer homomer , dimer
    HOMOLOGY
    interspecies homolog to yeast thioredoxin-dependent peroxide reductase (TPX)
    ortholog to Prdx2, Rattus norvegicus
    ortholog to Prdx2, Mus musculus
    homolog to drosophila Jafrac1
    ortholog to prdx2, Danio rerio
    ortholog to PRDX2, Pan troglodytes
    Homologene
    FAMILY
  • thioredoxin peroxidase family
  • peroxiredoxin protein family
  • ahpC/TSA family
  • CATEGORY enzyme
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm
    intracellular,nucleus
    text
  • strong cytoplasmic labeling in the basal cells of the corneal epithelial layer and the corneoscleral limbus
  • localized mainly in the nucleus of neural cells
  • basic FUNCTION
  • may be playing an important role in eliminating peroxides generated during metabolism
  • involved in redox regulation of the cell
  • reducing peroxides with reducing equivalents provided through the thioredoxin system
  • might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2)
  • enhancing natural killer (NK) cells activity
  • acting as a negative regulator of PDGF signaling
  • have a role in both the resistance of certain cancers to therapy and quite a different role in possibly slowing the progression of neurodegenerative diseases
  • functioning as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte and having nonredundant role in erythrocyte defense against oxidative stress
  • thiol-specific peroxidase, that regulate proinflammatory responses, vascular remodeling, and global oxidative stress
  • pecific peroxidase that inhibits atherogenic responses in vascular and inflammatory cells
  • has been shown to regulate diverse biological functions as cell proliferation and planar cell polarity, and also to affect wound healing
  • PRDX2 functions are modulated in response to oxidative stress in diseased Red blood cells
  • protects cells from deleterious oxidative damage
  • PRDX2 and PRDX4 are negative regulators of hypoxia-inducible factors under conditions of prolonged hypoxia
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    antioxidant
    a component
  • disulfide-linked homodimer
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • is a novel interacting partner to Hb in Red blood cells, the interaction of these two proteins could be construed as a novel form of PRDX2 protection against Hb instability
  • hyperoxidized PRDX2 interacts with the protein disulfide- isomerase TXNDC5
  • cell & other
    REGULATION
    Other phosphorylated by CDK5
    oxidized by endogenously generated H(2)O(2), which was mainly derived from hemoglobin autoxidation
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --low  
    induces neurodegeneration through oxidative damage, and enhancing Parkinson disease
    constitutional     --over  
    in end-stage dilated cardiomyopathy
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
  • may be potential targets for neuroprotective intervention in Parkinson's disease (
  • SystemTypeDisorderPubmed
    cardiovascularatheroma 
    specific activation of PRDX2 may be an effective means of antiatherogenic therapy
    ANIMAL & CELL MODELS
  • down-regulated PRDX2 through stable transfections of SH-SY5Y neuroblastoma cells with antisense contructs of the complete PRDX2 coding sequence display sensitivity to oxidative stress in addition to increased apoptosis under basal conditions and after treatment with oxidative cytotoxic agents (
  • PRX2 overexpression conferred marked in vitro and in vivo neuroprotection against 6-OHDA toxicity and anti-apoptotic effects in dopaminergic neurons, and preserved motor functions involving the dopamine system in mouse (
  • deficiency of Prdx2 in apolipoprotein E-deficient (ApoE(-/-) mice accelerated plaque formation with enhanced activation of RELA, JUN, JNKs, and MAPK14
  • loss of Prx II accelerates Heinz body formation by oxidative stress in mice, and increased Heinz body formation in Prx II-/- was mainly caused by denatured Hb aggregation