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Protein

Peroxiredoxin-1

Gene

PRDX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2 (PubMed:9497357). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).By similarity1 Publication

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei52Cysteine sulfenic acid (-SOH) intermediate2 Publications1

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • identical protein binding Source: Ensembl
  • peroxidase activity Source: MGI
  • RNA binding Source: UniProtKB
  • thioredoxin peroxidase activity Source: BHF-UCL

GO - Biological processi

  • cell proliferation Source: ProtInc
  • cell redox homeostasis Source: InterPro
  • cellular response to oxidative stress Source: Reactome
  • erythrocyte homeostasis Source: Ensembl
  • hydrogen peroxide catabolic process Source: BHF-UCL
  • natural killer cell activation Source: UniProtKB
  • natural killer cell mediated cytotoxicity Source: Ensembl
  • regulation of NF-kappaB import into nucleus Source: Ensembl
  • regulation of stress-activated MAPK cascade Source: Ensembl
  • removal of superoxide radicals Source: Ensembl
  • retina homeostasis Source: UniProtKB
  • skeletal system development Source: ProtInc

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-8862803. Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
SIGNORiQ06830.

Protein family/group databases

PeroxiBasei4501. Hs2CysPrx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-1 (EC:1.11.1.152 Publications)
Alternative name(s):
Natural killer cell-enhancing factor A
Short name:
NKEF-A
Proliferation-associated gene protein
Short name:
PAG
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Gene namesi
Name:PRDX1
Synonyms:PAGA, PAGB, TDPX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000117450.13.
HGNCiHGNC:9352. PRDX1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi90T → A: Abolishes phosphorylation by CDK1; 30% reduction in enzymatic activity. 1 Publication1
Mutagenesisi90T → D: 87% reduction in enzymatic activity. 1 Publication1

Organism-specific databases

DisGeNETi5052.
OpenTargetsiENSG00000117450.
PharmGKBiPA33722.

Chemistry databases

ChEMBLiCHEMBL5315.

Polymorphism and mutation databases

BioMutaiPRDX1.
DMDMi548453.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001350762 – 199Peroxiredoxin-1Add BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei7N6-acetyllysine; alternateCombined sources1
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei16N6-acetyllysineCombined sources1
Modified residuei27N6-acetyllysineCombined sources1
Modified residuei32PhosphoserineCombined sources1
Modified residuei35N6-acetyllysine; alternateCombined sources1
Modified residuei35N6-succinyllysine; alternateBy similarity1
Disulfide bondi52Interchain (with C-173); in linked formCombined sources1 Publication
Modified residuei90Phosphothreonine; by CDK11 Publication1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei136N6-acetyllysineBy similarity1
Disulfide bondi173Interchain (with C-52); in linked formCombined sources1 Publication
Cross-linki185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources

Post-translational modificationi

Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity.1 Publication
The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.6 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ06830.
MaxQBiQ06830.
PaxDbiQ06830.
PeptideAtlasiQ06830.
PRIDEiQ06830.
TopDownProteomicsiQ06830.

2D gel databases

DOSAC-COBS-2DPAGEiQ06830.
OGPiQ06830.
SWISS-2DPAGEiQ06830.
UCD-2DPAGEiQ06830.

PTM databases

iPTMnetiQ06830.
PhosphoSitePlusiQ06830.
SwissPalmiQ06830.

Expressioni

Inductioni

Constitutively expressed in most human cells; is induced to higher levels upon serum stimulation in untransformed and transformed cells.

Gene expression databases

BgeeiENSG00000117450.
CleanExiHS_PRDX1.
ExpressionAtlasiQ06830. baseline and differential.
GenevisibleiQ06830. HS.

Organism-specific databases

HPAiCAB004682.
HPA007730.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (PubMed:18172504). Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity). Interacts with SESN1 and SESN2 (PubMed:15105503).By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • identical protein binding Source: Ensembl

Protein-protein interaction databases

BioGridi111089. 133 interactors.
CORUMiQ06830.
DIPiDIP-33152N.
IntActiQ06830. 62 interactors.
MINTiMINT-4999060.
STRINGi9606.ENSP00000262746.

Structurei

Secondary structure

1199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Beta strandi16 – 20Combined sources5
Beta strandi26 – 30Combined sources5
Helixi31 – 34Combined sources4
Beta strandi37 – 43Combined sources7
Helixi48 – 50Combined sources3
Helixi54 – 61Combined sources8
Helixi63 – 68Combined sources6
Beta strandi71 – 79Combined sources9
Helixi81 – 88Combined sources8
Helixi92 – 94Combined sources3
Beta strandi104 – 106Combined sources3
Helixi111 – 115Combined sources5
Turni121 – 123Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi128 – 133Combined sources6
Beta strandi137 – 145Combined sources9
Helixi153 – 168Combined sources16
Beta strandi169 – 171Combined sources3
Helixi181 – 183Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RIIX-ray2.60A/B1-199[»]
3HY2X-ray2.10A/B1-199[»]
4XCSX-ray2.10A/B/C/D/E/F1-199[»]
ProteinModelPortaliQ06830.
SMRiQ06830.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06830.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 165ThioredoxinPROSITE-ProRule annotationAdd BLAST160

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOVERGENiHBG000286.
InParanoidiQ06830.
KOiK13279.
OMAiCPANWEE.
OrthoDBiEOG091G0IE5.
PhylomeDBiQ06830.
TreeFamiTF105181.

Family and domain databases

InterProiView protein in InterPro
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q06830-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF
60 70 80 90 100
VCPTEIIAFS DRAEEFKKLN CQVIGASVDS HFCHLAWVNT PKKQGGLGPM
110 120 130 140 150
NIPLVSDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITVNDLPVG
160 170 180 190
RSVDETLRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVQK SKEYFSKQK
Length:199
Mass (Da):22,110
Last modified:June 1, 1994 - v1
Checksum:i8F68E56D75BF5304
GO

Sequence cautioni

The sequence CAI13097 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti147L → P (PubMed:8026862).Curated1
Sequence conflicti149 – 150VG → CC (PubMed:8026862).Curated2
Sequence conflicti189Q → P (PubMed:8026862).Curated1
Sequence conflicti191S → T (PubMed:8026862).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02505062R → G1 PublicationCorresponds to variant dbSNP:rs34034070Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67951 mRNA. Translation: CAA48137.1.
L19184 mRNA. Translation: AAA50464.1.
BT019740 mRNA. Translation: AAV38545.1.
CR407652 mRNA. Translation: CAG28580.1.
DQ297142 Genomic DNA. Translation: ABB84465.1.
AB451262 mRNA. Translation: BAG70076.1.
AB451388 mRNA. Translation: BAG70202.1.
AL451136 Genomic DNA. Translation: CAI13095.1.
AL451136 Genomic DNA. Translation: CAI13096.1.
AL451136 Genomic DNA. Translation: CAI13097.1. Sequence problems.
CH471059 Genomic DNA. Translation: EAX06975.1.
CH471059 Genomic DNA. Translation: EAX06976.1.
CH471059 Genomic DNA. Translation: EAX06978.1.
CH471059 Genomic DNA. Translation: EAX06979.1.
CH471059 Genomic DNA. Translation: EAX06980.1.
CH471059 Genomic DNA. Translation: EAX06981.1.
CH471059 Genomic DNA. Translation: EAX06982.1.
BC007063 mRNA. Translation: AAH07063.1.
BC021683 mRNA. Translation: AAH21683.1.
CCDSiCCDS522.1.
PIRiA46711.
RefSeqiNP_001189360.1. NM_001202431.1.
NP_002565.1. NM_002574.3.
NP_859047.1. NM_181696.2.
NP_859048.1. NM_181697.2.
UniGeneiHs.180909.
Hs.731900.

Genome annotation databases

EnsembliENST00000262746; ENSP00000262746; ENSG00000117450.
ENST00000319248; ENSP00000361152; ENSG00000117450.
GeneIDi5052.
KEGGihsa:5052.
UCSCiuc001coa.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPRDX1_HUMAN
AccessioniPrimary (citable) accession number: Q06830
Secondary accession number(s): B5BU26
, D3DPZ8, P35703, Q2V576, Q5T154, Q5T155
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 27, 2017
This is version 197 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families