PRDX1 (peroxiredoxin 1)

2000-12-01   Jean-Loup Huret 

Identity

HGNC
LOCATION
1p34.1
LOCUSID
ALIAS
MSP23,NKEF-A,NKEFA,PAG,PAGA,PAGB,PRX1,PRXI,TDPX2
FUSION GENES

DNA/RNA

Description

6 exons, 13 kb

Transcription

937 bp mRNA; 599 bp coding sequence

Pseudogene

pseudogene in 9p22

Proteins

Description

199 amino acids; 22 kDa; form dimers through a disulfide bridge

Expression

widely expressed, in particular in the various cell types of the central nervous system and in red blood cells; overexpressed following induction of proliferation and oxidative stress

Localisation

cytosolic

Function

antioxidant, against oxidative stress; Abl SH3-binding protein; inhibitor of c-Abl tyrosine kinase activity; also binds to heme

Homology

thioperoxiredoxines

Implicated in

Disease
Correlations between the expression level and the stage of tumor progrssion in squamous cell carcinoma of the oral cavity; high expression in follicular thyroid tumors, but not in papillary carcinoma of the thyroid

Bibliography

Pubmed IDLast YearTitleAuthors
105359221999Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product.Hirotsu S et al
94973581998Characterization of a mammalian peroxiredoxin that contains one conserved cysteine.Kang SW et al
107296332000Peroxiredoxin I (macrophage 23 kDa stress protein) is highly and widely expressed in the rat nervous system.Mizusawa H et al
95068381998The pag gene product, a physiological inhibitor of c-abl tyrosine kinase, is overexpressed in cells entering S phase and by contact with agents inducing oxidative stress.Prospéri MT et al
104941091999Differential expression of peroxiredoxin subtypes in human brain cell types.Sarafian TA et al
86910791996Recombinant natural killer enhancing factor augments natural killer cytotoxicity.Sauri H et al
77026271995Antioxidant function of recombinant human natural killer enhancing factor.Sauri H et al
80268621994Cloning and sequence analysis of candidate human natural killer-enhancing factor genes.Shau H et al
81230501994Identification of natural killer enhancing factor as a major antioxidant in human red blood cells.Shau H et al
93343121997The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity.Wen ST et al
108401562000Peroxiredoxin I expression in oral cancer: a potential new tumor marker.Yanagawa T et al

Other Information

Locus ID:

NCBI: 5052
MIM: 176763
HGNC: 9352
Ensembl: ENSG00000117450

Variants:

dbSNP: 5052
ClinVar: 5052
TCGA: ENSG00000117450
COSMIC: PRDX1

RNA/Proteins

Gene IDTranscript IDUniprot
ENSG00000117450ENST00000262746Q06830
ENSG00000117450ENST00000262746A0A384NPQ2
ENSG00000117450ENST00000319248Q06830
ENSG00000117450ENST00000319248A0A384NPQ2
ENSG00000117450ENST00000372079A0A0A0MRQ5
ENSG00000117450ENST00000424390A0A0A0MSI0
ENSG00000117450ENST00000447184A0A0A0MSI0

Expression (GTEx)

0
100
200
300
400
500
600
700
800

Pathways

PathwaySourceExternal ID
PeroxisomeKEGGko04146
PeroxisomeKEGGhsa04146
DiseaseREACTOMER-HSA-1643685
Gene ExpressionREACTOMER-HSA-74160
Generic Transcription PathwayREACTOMER-HSA-212436
Transcriptional Regulation by TP53REACTOMER-HSA-3700989
TP53 Regulates Metabolic GenesREACTOMER-HSA-5628897
Cellular responses to stressREACTOMER-HSA-2262752
Detoxification of Reactive Oxygen SpeciesREACTOMER-HSA-3299685
Neurodegenerative DiseasesREACTOMER-HSA-8863678
Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease modelsREACTOMER-HSA-8862803

Protein levels (Protein atlas)

Not detected
Low
Medium
High

References

Pubmed IDYearTitleCitations
151055032004Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD.264
127147482003Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.144
121614452002Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid.135
154481642004Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine.124
186069872008HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation.103
119042902002Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site.88
229026302012Peroxiredoxin 1 functions as a signal peroxidase to receive, transduce, and transmit peroxide signals in mammalian cells.80
172347622007Human prx1 gene is a target of Nrf2 and is up-regulated by hypoxia/reoxygenation: implication to tumor biology.78
126509762003Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders.77
119863032002Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation.62

Citation

Jean-Loup Huret

PRDX1 (peroxiredoxin 1)

Atlas Genet Cytogenet Oncol Haematol. 2000-12-01

Online version: http://atlasgeneticsoncology.org/gene/266/prdx1

Historical Card

2000-10-01 PRDX1 (peroxiredoxin 1) by  Maité P Prosperi,Didier Ferbus,Gérard.Goubin 

Laboratoire dOncogenese, UMR147 CNRS, Section de recherche, Institut Curie, Paris, France.