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Protein

Glutathione peroxidase 2

Gene

GPX2

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

Functioni

Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors.

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei40 – 401

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB
  2. glutathione peroxidase activity Source: Reactome

GO - Biological processi

  1. interaction with symbiont Source: Ensembl
  2. negative regulation of inflammatory response to antigenic stimulus Source: Ensembl
  3. response to reactive oxygen species Source: Reactome
  4. response to symbiotic bacterium Source: Ensembl
  5. temperature homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciMetaCyc:HS11006-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150209. Synthesis of 5-eicosatetraenoic acids.
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_264249. Detoxification of Reactive Oxygen Species.
SABIO-RKP18283.

Protein family/group databases

PeroxiBasei3601. HsGPx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 2 (EC:1.11.1.9)
Short name:
GPx-2
Short name:
GSHPx-2
Alternative name(s):
Gastrointestinal glutathione peroxidase
Glutathione peroxidase-gastrointestinal
Short name:
GPx-GI
Short name:
GSHPx-GI
Glutathione peroxidase-related protein 2
Short name:
GPRP-2
Gene namesi
Name:GPX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:4554. GPX2.

Subcellular locationi

Cytoplasm
Note: Mainly cytoplasmic.

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28950.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Glutathione peroxidase 2PRO_0000066619Add
BLAST

Proteomic databases

MaxQBiP18283.
PaxDbiP18283.
PRIDEiP18283.

PTM databases

PhosphoSiteiP18283.

Expressioni

Tissue specificityi

Mostly in liver and gastrointestinal tract, not found in heart or kidney.

Gene expression databases

BgeeiP18283.
CleanExiHS_GPX2.
ExpressionAtlasiP18283. baseline and differential.
GenevestigatoriP18283.

Organism-specific databases

HPAiHPA003545.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi109135. 3 interactions.
IntActiP18283. 3 interactions.
STRINGi9606.ENSP00000374265.

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Beta strandi12 – 154Combined sources
Beta strandi20 – 223Combined sources
Helixi23 – 264Combined sources
Beta strandi29 – 368Combined sources
Helixi43 – 5614Combined sources
Turni58 – 603Combined sources
Beta strandi61 – 688Combined sources
Helixi79 – 813Combined sources
Helixi82 – 887Combined sources
Beta strandi98 – 1025Combined sources
Beta strandi105 – 1095Combined sources
Helixi114 – 1229Combined sources
Helixi137 – 1393Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi165 – 1695Combined sources
Helixi175 – 1784Combined sources
Helixi179 – 1868Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HE3X-ray2.10A4-188[»]
ProteinModelPortaliP18283.
SMRiP18283. Positions 4-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18283.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP18283.
KOiK00432.
OMAiPFKRYSK.
PhylomeDBiP18283.
TreeFamiTF105318.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18283-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLU GTTTRDFTQL
60 70 80 90 100
NELQCRFPRR LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT
110 120 130 140 150
LVQKCEVNGQ NEHPVFAYLK DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV
160 170 180 190
AWNFEKFLIG PEGEPFRRYS RTFPTINIEP DIKRLLKVAI
Length:190
Mass (Da):21,954
Last modified:February 26, 2008 - v3
Checksum:iFC8C4E69C4DE83A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371A → R in CAB43534 (PubMed:2388849).Curated
Sequence conflicti77 – 771C → S in CAB43534 (PubMed:2388849).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371A → L Requires 2 nucleotide substitutions. 1 Publication
VAR_003615
Natural varianti126 – 1261P → L.1 Publication
Corresponds to variant rs17881652 [ dbSNP | Ensembl ].
VAR_020916
Natural varianti146 – 1461R → C.1 Publication
Corresponds to variant rs17880492 [ dbSNP | Ensembl ].
VAR_020917
Natural varianti176 – 1761I → M.
VAR_003616

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei40 – 401Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53463 mRNA. Translation: CAB43534.1.
X68314 mRNA. Translation: CAA48394.1.
AF199441 Genomic DNA. Translation: AAF74026.1.
AY785560 Genomic DNA. Translation: AAV31780.1.
AL139022 Genomic DNA. No translation available.
BC005277 mRNA. Translation: AAH05277.1.
BC016756 mRNA. Translation: AAH16756.1.
BC022820 mRNA. Translation: AAH22820.2.
BC067221 mRNA. Translation: AAH67221.1.
CCDSiCCDS41964.1.
PIRiA45207.
RefSeqiNP_002074.2. NM_002083.3.
UniGeneiHs.2704.

Genome annotation databases

EnsembliENST00000389614; ENSP00000374265; ENSG00000176153.
GeneIDi2877.
KEGGihsa:2877.
UCSCiuc021ruq.2. human.

Polymorphism databases

DMDMi172046064.

Keywords - Coding sequence diversityi

Polymorphism, Selenocysteine

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53463 mRNA. Translation: CAB43534.1.
X68314 mRNA. Translation: CAA48394.1.
AF199441 Genomic DNA. Translation: AAF74026.1.
AY785560 Genomic DNA. Translation: AAV31780.1.
AL139022 Genomic DNA. No translation available.
BC005277 mRNA. Translation: AAH05277.1.
BC016756 mRNA. Translation: AAH16756.1.
BC022820 mRNA. Translation: AAH22820.2.
BC067221 mRNA. Translation: AAH67221.1.
CCDSiCCDS41964.1.
PIRiA45207.
RefSeqiNP_002074.2. NM_002083.3.
UniGeneiHs.2704.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HE3X-ray2.10A4-188[»]
ProteinModelPortaliP18283.
SMRiP18283. Positions 4-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109135. 3 interactions.
IntActiP18283. 3 interactions.
STRINGi9606.ENSP00000374265.

Chemistry

DrugBankiDB00143. Glutathione.

Protein family/group databases

PeroxiBasei3601. HsGPx02.

PTM databases

PhosphoSiteiP18283.

Polymorphism databases

DMDMi172046064.

Proteomic databases

MaxQBiP18283.
PaxDbiP18283.
PRIDEiP18283.

Protocols and materials databases

DNASUi2877.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389614; ENSP00000374265; ENSG00000176153.
GeneIDi2877.
KEGGihsa:2877.
UCSCiuc021ruq.2. human.

Organism-specific databases

CTDi2877.
GeneCardsiGC14M065405.
H-InvDBHIX0037716.
HGNCiHGNC:4554. GPX2.
HPAiHPA003545.
MIMi138319. gene.
neXtProtiNX_P18283.
PharmGKBiPA28950.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP18283.
KOiK00432.
OMAiPFKRYSK.
PhylomeDBiP18283.
TreeFamiTF105318.

Enzyme and pathway databases

BioCyciMetaCyc:HS11006-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150209. Synthesis of 5-eicosatetraenoic acids.
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_264249. Detoxification of Reactive Oxygen Species.
SABIO-RKP18283.

Miscellaneous databases

EvolutionaryTraceiP18283.
GeneWikiiGPX2_(gene).
GenomeRNAii2877.
NextBioi11359.
PROiP18283.
SOURCEiSearch...

Gene expression databases

BgeeiP18283.
CleanExiHS_GPX2.
ExpressionAtlasiP18283. baseline and differential.
GenevestigatoriP18283.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human cDNA sequence of a novel glutathione peroxidase-related protein."
    Akasaka M., Mizoguchi J., Takahashi K.
    Nucleic Acids Res. 18:4619-4619(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI."
    Chu F.-F., Doroshow J.H., Esworthy R.S.
    J. Biol. Chem. 268:2571-2576(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Liver.
  3. "Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents."
    Kelner M.J., Bagnell R.D., Montoya M.A., Lanham K.A.
    Gene 248:109-116(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-37.
  4. NIEHS SNPs program
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-126 AND CYS-146.
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain, Prostate and Urinary bladder.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Crystal structure of the selenocysteine to cysteine mutant of human glutathione peroxidase 2 (GPX2)."
    Structural genomics consortium (SGC)
    Submitted (JAN-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4-188.

Entry informationi

Entry nameiGPX2_HUMAN
AccessioniPrimary (citable) accession number: P18283
Secondary accession number(s): Q6PJ52, Q8WWI7, Q9NRP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 26, 2008
Last modified: April 1, 2015
This is version 148 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

External Data

Dasty 3

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 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.