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Protein

Glutathione peroxidase 1

Gene

GPX1

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

Functioni

Protects the hemoglobin in erythrocytes from oxidative breakdown.

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei491
Sitei49Subject to oxidation and hydroselenide loss to dehydroalanineBy similarity1

GO - Molecular functioni

  • glutathione peroxidase activity Source: BHF-UCL
  • SH3 domain binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciMetaCyc:HS00019-MONOMER.
ZFISH:HS00019-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-2142688. Synthesis of 5-eicosatetraenoic acids.
R-HSA-2142712. Synthesis of 12-eicosatetraenoic acid derivatives.
R-HSA-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-74259. Purine catabolism.
SIGNORiP07203.

Protein family/group databases

PeroxiBasei3600. HsGPx01-A.

Chemistry databases

SwissLipidsiSLP:000001632.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 1 (EC:1.11.1.9)
Short name:
GPx-1
Short name:
GSHPx-1
Alternative name(s):
Cellular glutathione peroxidase
Gene namesi
Name:GPX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:4553. GPX1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi2876.
MalaCardsiGPX1.
MIMi138320. gene+phenotype.
OpenTargetsiENSG00000233276.
PharmGKBiPA28949.

Chemistry databases

ChEMBLiCHEMBL2163186.
DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGPX1.
DMDMi311033481.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000666101 – 203Glutathione peroxidase 1Add BLAST203

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34PhosphoserineBy similarity1
Modified residuei88N6-acetyllysine; alternateBy similarity1
Modified residuei88N6-succinyllysine; alternateBy similarity1
Modified residuei114N6-acetyllysine; alternateBy similarity1
Modified residuei114N6-succinyllysine; alternateBy similarity1
Modified residuei148N6-acetyllysine; alternateBy similarity1
Modified residuei148N6-succinyllysine; alternateBy similarity1
Modified residuei197PhosphoserineBy similarity1
Modified residuei201PhosphoserineCombined sources1

Post-translational modificationi

During periods of oxidative stress, Sec-49 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP07203.
PaxDbiP07203.
PeptideAtlasiP07203.
PRIDEiP07203.

2D gel databases

OGPiP07203.
SWISS-2DPAGEP07203.

PTM databases

iPTMnetiP07203.
PhosphoSitePlusiP07203.
SwissPalmiP07203.

Expressioni

Gene expression databases

BgeeiENSG00000233276.
CleanExiHS_GPX1.
ExpressionAtlasiP07203. baseline and differential.
GenevisibleiP07203. HS.

Organism-specific databases

HPAiCAB011582.
HPA044758.

Interactioni

Subunit structurei

Homotetramer. Interacts with MIEN1.

GO - Molecular functioni

  • SH3 domain binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109134. 15 interactors.
IntActiP07203. 9 interactors.
STRINGi9606.ENSP00000407375.

Chemistry databases

BindingDBiP07203.

Structurei

Secondary structure

1203
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 18Combined sources3
Helixi32 – 35Combined sources4
Beta strandi38 – 45Combined sources8
Beta strandi47 – 49Combined sources3
Helixi52 – 66Combined sources15
Helixi67 – 69Combined sources3
Beta strandi71 – 77Combined sources7
Turni82 – 85Combined sources4
Helixi89 – 91Combined sources3
Helixi92 – 98Combined sources7
Beta strandi108 – 112Combined sources5
Helixi124 – 132Combined sources9
Helixi147 – 149Combined sources3
Beta strandi152 – 154Combined sources3
Beta strandi166 – 169Combined sources4
Beta strandi175 – 179Combined sources5
Helixi185 – 188Combined sources4
Helixi189 – 196Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F8AX-ray1.50A/B14-198[»]
ProteinModelPortaliP07203.
SMRiP07203.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07203.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP07203.
KOiK00432.
OMAiCEVNGEK.
OrthoDBiEOG091G10LN.
PhylomeDBiP07203.
TreeFamiTF105318.

Family and domain databases

CDDicd00340. GSH_Peroxidase. 1 hit.
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]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P07203-1) [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
MCAARLAAAA AAAQSVYAFS ARPLAGGEPV SLGSLRGKVL LIENVASLUG
60 70 80 90 100
TTVRDYTQMN ELQRRLGPRG LVVLGFPCNQ FGHQENAKNE EILNSLKYVR
110 120 130 140 150
PGGGFEPNFM LFEKCEVNGA GAHPLFAFLR EALPAPSDDA TALMTDPKLI
160 170 180 190 200
TWSPVCRNDV AWNFEKFLVG PDGVPLRRYS RRFQTIDIEP DIEALLSQGP

SCA
Length:203
Mass (Da):22,088
Last modified:November 2, 2010 - v4
Checksum:i5DB11579C66FE8E5
GO
Isoform 2 (identifier: P07203-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-98: ENAKNEEILNSLKY → VRRAERGGAGADVQ
     99-203: Missing.

Note: Gene prediction based on EST data.
Show »
Length:98
Mass (Da):10,289
Checksum:i9AD713E53537E4A0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti93L → Q in CAA31992 (PubMed:2955287).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0209125R → P.1 PublicationCorresponds to variant rs8179169dbSNPEnsembl.1
Natural variantiVAR_0209137 – 8Missing .5 Publications2
Natural variantiVAR_0209148Missing .3 Publications1
Natural variantiVAR_020915194A → T.1 PublicationCorresponds to variant rs6446261dbSNPEnsembl.1
Natural variantiVAR_007904200P → L Frequent polymorphism. 4 PublicationsCorresponds to variant rs1050450dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04736985 – 98ENAKN…NSLKY → VRRAERGGAGADVQ in isoform 2. CuratedAdd BLAST14
Alternative sequenceiVSP_04737099 – 203Missing in isoform 2. CuratedAdd BLAST105

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei49Selenocysteine1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00433 mRNA. Translation: CAA68491.1.
Y00483 Genomic DNA. Translation: CAB37833.1.
X13709 mRNA. Translation: CAA31992.1.
X13710 mRNA. Translation: CAA31993.1.
M21304 mRNA. Translation: AAA75389.2.
M83094 Genomic DNA. Translation: AAA67540.2.
AY327818 Genomic DNA. Translation: AAP80181.1.
AC121247 Genomic DNA. No translation available.
BC000742 mRNA. Translation: AAH00742.3.
CCDSiCCDS43091.1. [P07203-1]
CCDS54582.1. [P07203-2]
PIRiA42152. OPHUE.
RefSeqiNP_000572.2. NM_000581.3. [P07203-1]
UniGeneiHs.76686.

Genome annotation databases

EnsembliENST00000419349; ENSP00000391316; ENSG00000233276. [P07203-2]
ENST00000419783; ENSP00000407375; ENSG00000233276. [P07203-1]
GeneIDi2876.
KEGGihsa:2876.
UCSCiuc021wxw.2. human. [P07203-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Selenocysteine

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Glutathione peroxidase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00433 mRNA. Translation: CAA68491.1.
Y00483 Genomic DNA. Translation: CAB37833.1.
X13709 mRNA. Translation: CAA31992.1.
X13710 mRNA. Translation: CAA31993.1.
M21304 mRNA. Translation: AAA75389.2.
M83094 Genomic DNA. Translation: AAA67540.2.
AY327818 Genomic DNA. Translation: AAP80181.1.
AC121247 Genomic DNA. No translation available.
BC000742 mRNA. Translation: AAH00742.3.
CCDSiCCDS43091.1. [P07203-1]
CCDS54582.1. [P07203-2]
PIRiA42152. OPHUE.
RefSeqiNP_000572.2. NM_000581.3. [P07203-1]
UniGeneiHs.76686.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F8AX-ray1.50A/B14-198[»]
ProteinModelPortaliP07203.
SMRiP07203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109134. 15 interactors.
IntActiP07203. 9 interactors.
STRINGi9606.ENSP00000407375.

Chemistry databases

BindingDBiP07203.
ChEMBLiCHEMBL2163186.
DrugBankiDB00143. Glutathione.
SwissLipidsiSLP:000001632.

Protein family/group databases

PeroxiBasei3600. HsGPx01-A.

PTM databases

iPTMnetiP07203.
PhosphoSitePlusiP07203.
SwissPalmiP07203.

Polymorphism and mutation databases

BioMutaiGPX1.
DMDMi311033481.

2D gel databases

OGPiP07203.
SWISS-2DPAGEP07203.

Proteomic databases

EPDiP07203.
PaxDbiP07203.
PeptideAtlasiP07203.
PRIDEiP07203.

Protocols and materials databases

DNASUi2876.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000419349; ENSP00000391316; ENSG00000233276. [P07203-2]
ENST00000419783; ENSP00000407375; ENSG00000233276. [P07203-1]
GeneIDi2876.
KEGGihsa:2876.
UCSCiuc021wxw.2. human. [P07203-1]

Organism-specific databases

CTDi2876.
DisGeNETi2876.
GeneCardsiGPX1.
H-InvDBHIX0003298.
HGNCiHGNC:4553. GPX1.
HPAiCAB011582.
HPA044758.
MalaCardsiGPX1.
MIMi138320. gene+phenotype.
neXtProtiNX_P07203.
OpenTargetsiENSG00000233276.
PharmGKBiPA28949.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP07203.
KOiK00432.
OMAiCEVNGEK.
OrthoDBiEOG091G10LN.
PhylomeDBiP07203.
TreeFamiTF105318.

Enzyme and pathway databases

BioCyciMetaCyc:HS00019-MONOMER.
ZFISH:HS00019-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-2142688. Synthesis of 5-eicosatetraenoic acids.
R-HSA-2142712. Synthesis of 12-eicosatetraenoic acid derivatives.
R-HSA-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-74259. Purine catabolism.
SIGNORiP07203.

Miscellaneous databases

ChiTaRSiGPX1. human.
EvolutionaryTraceiP07203.
GeneWikiiGPX1.
GenomeRNAii2876.
PROiP07203.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000233276.
CleanExiHS_GPX1.
ExpressionAtlasiP07203. baseline and differential.
GenevisibleiP07203. HS.

Family and domain databases

CDDicd00340. GSH_Peroxidase. 1 hit.
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...

Entry informationi

Entry nameiGPX1_HUMAN
AccessioniPrimary (citable) accession number: P07203
Secondary accession number(s): E9PAS1, Q7Z5H1, Q9BW12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 2, 2010
Last modified: November 30, 2016
This is version 195 of the entry and version 4 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 3
    Human chromosome 3: 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.