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0PRDX2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePRDX2
DescriptionPeroxiredoxin 2 (ec 1.11.1.15) (thioredoxin peroxidase 1) (thioredoxin-dependent peroxide reductase 1) (thiol-specific antioxidant protein) (tsa) (prp) (natural killer cell enhancing factor b) (nkef-b).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016209 antioxidant activity (NAS)
0005489 electron transporter activity (TAS)
0008379 thioredoxin peroxidase activity (TAS)
0042981 regulation of apoptosis (IMP)
0006979 response to oxidative stress (IMP)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels which mediate signal transduction in mammalian cells. Prxs can be regulated by changes to phosphorylation.edox and possibly oligomerization states. Prxs are divided into three classes: typical 2-Cys Prxs; atypical 2-Cys Prxs; and 1-Cys Prxs. All Prxs share the same basic catalytic mechanism.n which an active-site cysteine (the peroxidatic cysteine) is oxidized to a sulphenic acid by the peroxide substrate. The recycling of the sulphenic acid back to a thiol is what distinguishes the three enzyme classes. Using crystal structures. detailed catalytic cycle has been derived for typical 2-Cys Prxs.ncluding a model for the redox-regulated oligomeric state proposed to control enzyme activity .Alkyl hydroperoxide reductase (AhpC) is responsible for directly reducing organic hyperoxides in its reduced dithiol form. Thiol specific antioxidant (TSA) is a physiologically important antioxidantwhich constitutes an enzymatic defense against sulphur-containing radicals. This family contains AhpC and TSA.s well as related proteins.Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen.tings.rugs.r food) that.n most people.esult in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P..offmann D..oewenstein H..arsh D.G..latts-Mills T.A.E..homas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed ofthe first three letters of the genus; a space; the first letter of thespecies name; a space and an arabic number. In the event that two speciesnames have identical designations.hey are discriminated from one anotherby adding one or more letters (as necessary) to each species designation. The allergens in this family include allergens with the following designations: Asp f 3.al f 2 and Mal f 3.
  IPR000866:Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen
Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2).here a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system.he NADP/thioredoxin system.nd the glutathione/glutaredoxin system . Several of these disulphide proteins share a common structure.onsisting of a three-layer alpha/beta/alpha core. Proteins that contain this thioredoxin fold include: 2Fe-2S ferredoxin.hioltransferase.hosducin.lutathione peroxidase-like enzymes.rsenate reductase.isulphide bond isomerase DsbC (C-terminal domain).isulphide bond facilitator DsbA (contains an alpha-helical insertion).lutathione S-transferase (N-terminal domain).ndoplasmic reticulum protein ERP29 (N-terminal domain).pliceosomal protein U5-15Kd.ircadian oscillation regulator KaiB.rotein disulphide isomerase PDI (contains two tandem repeats of this fold).nd calsequestrin (contains three tandem repeats of this fold).This entry differs from the thioredoxin-like fold protein.he classification of this fold in glutathione S-transferase enzymes.here this entry defines two regions containing this fold.nd the thioredoxin-like fold protein defines only the N-terminal as containing this fold.
  IPR012335:Thioredoxin fold
Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2).here a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system.he NADP/thioredoxin system.nd the glutathione/glutaredoxin system . Several of these disulphide proteins share a common structure.onsisting of a three-layer alpha/beta/alpha core. Proteins that contain this thioredoxin fold include: 2Fe-2S ferredoxin.hioltransferase.hosducin.lutathione peroxidase-like enzymes.rsenate reductase.isulphide bond isomerase DsbC (C-terminal domain).isulphide bond facilitator DsbA (contains an alpha-helical insertion).lutathione S-transferase (N-terminal domain).ndoplasmic reticulum protein ERP29 (N-terminal domain).pliceosomal protein U5-15Kd.ircadian oscillation regulator KaiB.rotein disulphide isomerase PDI (contains two tandem repeats of this fold).nd calsequestrin (contains three tandem repeats of this fold).This entry differs from the thioredoxin fold protein.he classification of this fold is in the glutathione S-transferase enzymes.here this entry defines two regions containing this fold.nd the thioredoxin fold protein defines only the N-terminal as containing this fold.
  IPR012336:Thioredoxin-like fold
IPR000866:AhpC-TSA 
Evalue:-129.292434692383 
Location:7-184
SequencesProtein: PRDX2_HUMAN (197 aa)
mRNA: NM_005809
Local Annotation
Synapse Ontology
Microglias, one kind of glias in CNS, are responsible for removing most of the waste and cellular debris from the CNS
sdb:0267 removing metabolic mass  (Evidence:keywords)
KO assignmentK03386
  Level 3 annotation:
    peroxiredoxin (alkyl hydroperoxide reductase subunit C)
  Level 2 annotation:
    Protein folding and associated processing
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 116 residues, 12768634-12768980Exon2: 45 residues, 12771672-12771803Exon3: 43 residues, 12771990-12772113Exon4: 53 residues, 12772729-12772883Exon5: 39 residues, 12772972-12773084Exon6: 49 residues, 12773553-12773694Exon7: 2 residues, -Jump to PRDX2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4368 12768634-12773694 ~-5K 18105(PRDX2)(-)Loci: 3091 12810347-12846765 ~-36K 18111(MAST1)(+)Loci: 3092 12862973-12871782 ~-9K 18114(GCDH)(+)Loci: 4369 13115902-13122052 ~-6K 18133(STX10)(-)Loci: 4370 13179114-13478317 ~-299K 18136(CACNA1A)(-)Loci: 4367 12734816-12747337 ~-13K 18101(HOOK2)(-)Link out to UCSC