MGP Database

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MGP002193

UniProt Annotations

Entry Information
Gene Nameperoxiredoxin 1
Protein EntryPRDX1_HUMAN
UniProt IDQ06830
SpeciesHuman
Comments
Comment typeDescription
Catalytic Activity2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
FunctionInvolved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not 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). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). {ECO:0000250}.
InductionConstitutively expressed in most human cells; is induced to higher levels upon serum stimulation in untransformed and transformed cells.
InteractionP10275:AR; NbExp=3; IntAct=EBI-353193, EBI-608057; P60484:PTEN; NbExp=7; IntAct=EBI-353193, EBI-696162;
MiscellaneousInactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized.
MiscellaneousThe active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.
PtmPhosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity. {ECO:0000269|PubMed:11986303}.
Sequence CautionSequence=CAI13097.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
SimilarityBelongs to the AhpC/TSA family. {ECO:0000305}.
SimilarityContains 1 thioredoxin domain. {ECO:0000255|PROSITE- ProRule:PRU00691}.
Subcellular LocationCytoplasm {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
SubunitHomodimer; disulfide-linked, upon oxidation (By similarity). May form heterodimers with AOP2. Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity). {ECO:0000250}.
Web ResourceName=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/PAGID266.html";
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/prdx1/";
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