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Protein

Peroxiredoxin-2

Gene

PRDX2

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

Functioni

Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons 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 H2O2.

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei51Cysteine sulfenic acid (-SOH) intermediate1

GO - Molecular functioni

  • antioxidant activity Source: UniProtKB
  • thioredoxin peroxidase activity Source: UniProtKB

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular response to oxidative stress Source: BHF-UCL
  • hydrogen peroxide catabolic process Source: BHF-UCL
  • negative regulation of apoptotic process Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • removal of superoxide radicals Source: BHF-UCL
  • response to oxidative stress Source: UniProtKB
  • response to reactive oxygen species Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciZFISH:HS09645-MONOMER.
BRENDAi1.11.1.15. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-5628897. TP53 Regulates Metabolic Genes.

Protein family/group databases

PeroxiBasei4475. Hs2CysPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-2 (EC:1.11.1.15)
Alternative name(s):
Natural killer cell-enhancing factor B
Short name:
NKEF-B
PRP
Thiol-specific antioxidant protein
Short name:
TSA
Thioredoxin peroxidase 1
Thioredoxin-dependent peroxide reductase 1
Gene namesi
Name:PRDX2
Synonyms:NKEFB, TDPX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9353. PRDX2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi7001.
OpenTargetsiENSG00000167815.
PharmGKBiPA33723.

Polymorphism and mutation databases

DMDMi2507169.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001350802 – 198Peroxiredoxin-2Add BLAST197

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Disulfide bondi51Interchain (with C-172); in linked formBy similarity
Modified residuei112PhosphoserineCombined sources1
Disulfide bondi172Interchain (with C-51); in linked formBy similarity
Modified residuei182PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP32119.
PaxDbiP32119.
PeptideAtlasiP32119.
PRIDEiP32119.
TopDownProteomicsiP32119-1. [P32119-1]

2D gel databases

DOSAC-COBS-2DPAGEP32119.
OGPiP32119.
REPRODUCTION-2DPAGEIPI00027350.
SWISS-2DPAGEP32119.
UCD-2DPAGEP32119.

PTM databases

iPTMnetiP32119.
PhosphoSitePlusiP32119.
SwissPalmiP32119.

Expressioni

Gene expression databases

BgeeiENSG00000167815.
CleanExiHS_PRDX2.
ExpressionAtlasiP32119. baseline and differential.
GenevisibleiP32119. HS.

Organism-specific databases

HPAiCAB008713.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. May be found as a toroid-shaped decamer composed of 5 dimers, depending on pH and calcium concentration. Interacts with TIPIN.1 Publication

Protein-protein interaction databases

BioGridi112860. 98 interactors.
DIPiDIP-39882N.
IntActiP32119. 44 interactors.
MINTiMINT-3012817.
STRINGi9606.ENSP00000301522.

Structurei

Secondary structure

1198
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 21Combined sources6
Beta strandi24 – 29Combined sources6
Helixi30 – 33Combined sources4
Beta strandi36 – 42Combined sources7
Helixi50 – 60Combined sources11
Helixi62 – 66Combined sources5
Turni67 – 69Combined sources3
Beta strandi70 – 78Combined sources9
Helixi80 – 87Combined sources8
Helixi91 – 93Combined sources3
Beta strandi103 – 105Combined sources3
Helixi110 – 114Combined sources5
Turni120 – 122Combined sources3
Beta strandi127 – 132Combined sources6
Beta strandi136 – 144Combined sources9
Helixi152 – 168Combined sources17
Helixi187 – 197Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QMVX-ray1.70A/B/C/D/E/F/G/H/I/J2-198[»]
ProteinModelPortaliP32119.
SMRiP32119.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32119.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 164ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP32119.
KOiK03386.
OMAiDYEVVHE.
OrthoDBiEOG091G0IE5.
PhylomeDBiP32119.
TreeFamiTF105181.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR033046. PRDX2.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10681:SF124. PTHR10681:SF124. 1 hit.
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P32119-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV
60 70 80 90 100
CPTEIIAFSN RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN
110 120 130 140 150
IPLLADVTRR LSEDYGVLKT DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR
160 170 180 190
SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN
Length:198
Mass (Da):21,892
Last modified:January 23, 2007 - v5
Checksum:i1AC781D908B32B46
GO
Isoform 2 (identifier: P32119-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-198: INTPRKEGGL...DSKEYFSKHN → YEQGPKREVA...SLRMMTVISI

Note: No experimental confirmation available. Due to intron retention. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:142
Mass (Da):15,819
Checksum:iC1FE1157EED6EC5E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti59 – 66SNRAEDFR → TTVKRTSA in CAA80269 (PubMed:8144038).Curated8
Sequence conflicti82T → N in AAA50465 (PubMed:8026862).Curated1
Sequence conflicti105A → G in AAA50465 (PubMed:8026862).Curated1
Sequence conflicti120T → N in CAA80269 (PubMed:8144038).Curated1
Sequence conflicti126 – 127YR → TT AA sequence (PubMed:8313871).Curated2
Sequence conflicti175G → A in CAA80269 (PubMed:8144038).Curated1
Sequence conflicti180S → R in CAA80269 (PubMed:8144038).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025051153D → E.1 PublicationCorresponds to variant rs34012472dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04292487 – 198INTPR…FSKHN → YEQGPKREVAAKLTPSGPSS VASWPLLNLWNLRFPIVKIM ETLPPKSLRMMTVISI in isoform 2. 1 PublicationAdd BLAST112

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22548 mRNA. Translation: CAA80269.1.
L19185 mRNA. Translation: AAA50465.1.
CR450356 mRNA. Translation: CAG29352.1.
CR541789 mRNA. Translation: CAG46588.1.
AK289485 mRNA. Translation: BAF82174.1.
DQ231563 Genomic DNA. Translation: ABB02182.1.
AC018761 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84311.1.
BC000452 mRNA. Translation: AAH00452.1.
BC003022 mRNA. Translation: AAH03022.1.
BC039428 mRNA. Translation: AAH39428.1.
X82321 mRNA. Translation: CAA57764.1.
CCDSiCCDS12281.1. [P32119-1]
PIRiI68897.
RefSeqiNP_005800.3. NM_005809.5. [P32119-1]
UniGeneiHs.432121.

Genome annotation databases

EnsembliENST00000301522; ENSP00000301522; ENSG00000167815. [P32119-1]
GeneIDi7001.
KEGGihsa:7001.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22548 mRNA. Translation: CAA80269.1.
L19185 mRNA. Translation: AAA50465.1.
CR450356 mRNA. Translation: CAG29352.1.
CR541789 mRNA. Translation: CAG46588.1.
AK289485 mRNA. Translation: BAF82174.1.
DQ231563 Genomic DNA. Translation: ABB02182.1.
AC018761 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84311.1.
BC000452 mRNA. Translation: AAH00452.1.
BC003022 mRNA. Translation: AAH03022.1.
BC039428 mRNA. Translation: AAH39428.1.
X82321 mRNA. Translation: CAA57764.1.
CCDSiCCDS12281.1. [P32119-1]
PIRiI68897.
RefSeqiNP_005800.3. NM_005809.5. [P32119-1]
UniGeneiHs.432121.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QMVX-ray1.70A/B/C/D/E/F/G/H/I/J2-198[»]
ProteinModelPortaliP32119.
SMRiP32119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112860. 98 interactors.
DIPiDIP-39882N.
IntActiP32119. 44 interactors.
MINTiMINT-3012817.
STRINGi9606.ENSP00000301522.

Protein family/group databases

PeroxiBasei4475. Hs2CysPrx02.

PTM databases

iPTMnetiP32119.
PhosphoSitePlusiP32119.
SwissPalmiP32119.

Polymorphism and mutation databases

DMDMi2507169.

2D gel databases

DOSAC-COBS-2DPAGEP32119.
OGPiP32119.
REPRODUCTION-2DPAGEIPI00027350.
SWISS-2DPAGEP32119.
UCD-2DPAGEP32119.

Proteomic databases

EPDiP32119.
PaxDbiP32119.
PeptideAtlasiP32119.
PRIDEiP32119.
TopDownProteomicsiP32119-1. [P32119-1]

Protocols and materials databases

DNASUi7001.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301522; ENSP00000301522; ENSG00000167815. [P32119-1]
GeneIDi7001.
KEGGihsa:7001.

Organism-specific databases

CTDi7001.
DisGeNETi7001.
GeneCardsiPRDX2.
HGNCiHGNC:9353. PRDX2.
HPAiCAB008713.
MIMi600538. gene.
neXtProtiNX_P32119.
OpenTargetsiENSG00000167815.
PharmGKBiPA33723.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP32119.
KOiK03386.
OMAiDYEVVHE.
OrthoDBiEOG091G0IE5.
PhylomeDBiP32119.
TreeFamiTF105181.

Enzyme and pathway databases

BioCyciZFISH:HS09645-MONOMER.
BRENDAi1.11.1.15. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

ChiTaRSiPRDX2. human.
EvolutionaryTraceiP32119.
GeneWikiiPeroxiredoxin_2.
GenomeRNAii7001.
PROiP32119.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000167815.
CleanExiHS_PRDX2.
ExpressionAtlasiP32119. baseline and differential.
GenevisibleiP32119. HS.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR033046. PRDX2.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10681:SF124. PTHR10681:SF124. 1 hit.
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRDX2_HUMAN
AccessioniPrimary (citable) accession number: P32119
Secondary accession number(s): A8K0C0
, P31945, P32118, P35701, Q6FHG4, Q92763, Q9UC23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 193 of the entry and version 5 of the sequence. [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

Miscellaneous

The active site is the redox-active Cys-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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.
Inactivated upon oxidative stress by overoxidation of Cys-51 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized.

Keywords - Technical termi

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

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.