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UniProtKB - P32119 (PRDX2_HUMAN)

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Protein

Peroxiredoxin-2

Gene

PRDX2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 H2O2.1 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 sitei51Cysteine sulfenic acid (-SOH) intermediate1 Publication1

GO - Molecular functioni

  • antioxidant activity Source: UniProtKB
  • thioredoxin peroxidase activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

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
View the complete GO annotation on QuickGO ...

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

Protein family/group databases

PeroxiBasei4475 Hs2CysPrx02

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-2 (EC:1.11.1.152 Publications)
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000167815.11
HGNCiHGNC:9353 PRDX2
MIMi600538 gene
neXtProtiNX_P32119

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

Organism-specific databases

DisGeNETi7001
OpenTargetsiENSG00000167815
PharmGKBiPA33723

Chemistry databases

DrugBankiDB02153 3-Sulfinoalanine
DB04048 N-Carbamoyl-Alanine

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 formCombined sources1 Publication
Modified residuei112PhosphoserineCombined sources1
Disulfide bondi172Interchain (with C-51); in linked formCombined sources1 Publication
Modified residuei182PhosphothreonineCombined sources1

Post-translational modificationi

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.By similarity2 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP32119
PaxDbiP32119
PeptideAtlasiP32119
PRIDEiP32119
ProteomicsDBi54836
54837 [P32119-2]
TopDownProteomicsiP32119-1 [P32119-1]

2D gel databases

DOSAC-COBS-2DPAGEiP32119
OGPiP32119
REPRODUCTION-2DPAGEiIPI00027350
SWISS-2DPAGEiP32119
UCD-2DPAGEiP32119

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 (PubMed:27892488). 5 homodimers assemble to form a ring-like decamer (PubMed:27892488). Interacts with TIPIN (PubMed:17141802).2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi112860, 128 interactors
DIPiDIP-39882N
IntActiP32119, 47 interactors
MINTiP32119
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 strandi123 – 125Combined sources3
Beta strandi127 – 132Combined sources6
Beta strandi136 – 144Combined sources9
Helixi152 – 168Combined sources17
Helixi187 – 197Combined sources11

3D structure databases

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 peroxiredoxin family. AhpC/Prx1 subfamily.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR000866 AhpC/TSA
IPR024706 Peroxiredoxin_AhpC-typ
IPR019479 Peroxiredoxin_C
IPR036249 Thioredoxin-like_sf
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

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 → E1 PublicationCorresponds to variant dbSNP:rs34012472Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiPRDX2_HUMAN
AccessioniPrimary (citable) accession number: P32119
Secondary accession number(s): A8K0C0
, P31945, P32118, P35701, Q6FHG4, Q92763, Q9UC23
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 210 of the entry and version 5 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 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

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