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P07203

- GPX1_HUMAN

UniProt

P07203 - GPX1_HUMAN

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Protein

Glutathione peroxidase 1

Gene

GPX1

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491
Sitei49 – 491Subject to oxidation and hydroselenide loss to dehydroalanineBy similarity

GO - Molecular functioni

  1. glutathione binding Source: Ensembl
  2. glutathione peroxidase activity Source: BHF-UCL
  3. phospholipid-hydroperoxide glutathione peroxidase activity Source: Ensembl
  4. selenium binding Source: Ensembl
  5. SH3 domain binding Source: BHF-UCL

GO - Biological processi

  1. aging Source: Ensembl
  2. angiogenesis involved in wound healing Source: Ensembl
  3. arachidonic acid metabolic process Source: Reactome
  4. blood vessel endothelial cell migration Source: Ensembl
  5. cell redox homeostasis Source: BHF-UCL
  6. cellular response to oxidative stress Source: ParkinsonsUK-UCL
  7. endothelial cell development Source: Ensembl
  8. fat cell differentiation Source: Ensembl
  9. glutathione metabolic process Source: BHF-UCL
  10. heart contraction Source: BHF-UCL
  11. hydrogen peroxide catabolic process Source: BHF-UCL
  12. interaction with symbiont Source: Ensembl
  13. intrinsic apoptotic signaling pathway in response to oxidative stress Source: Ensembl
  14. lipoxygenase pathway Source: Reactome
  15. myoblast proliferation Source: Ensembl
  16. negative regulation of apoptotic process Source: Ensembl
  17. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  18. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  19. negative regulation of inflammatory response to antigenic stimulus Source: Ensembl
  20. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
  21. negative regulation of release of cytochrome c from mitochondria Source: BHF-UCL
  22. nucleobase-containing small molecule metabolic process Source: Reactome
  23. positive regulation of fibril organization Source: ParkinsonsUK-UCL
  24. positive regulation of protein kinase B signaling Source: Ensembl
  25. protein oxidation Source: Ensembl
  26. purine nucleobase metabolic process Source: Reactome
  27. purine nucleotide catabolic process Source: Reactome
  28. regulation of gene expression, epigenetic Source: BHF-UCL
  29. regulation of mammary gland epithelial cell proliferation Source: BHF-UCL
  30. regulation of neuron apoptotic process Source: Ensembl
  31. regulation of proteasomal protein catabolic process Source: BHF-UCL
  32. response to estradiol Source: Ensembl
  33. response to folic acid Source: Ensembl
  34. response to gamma radiation Source: Ensembl
  35. response to glucose Source: Ensembl
  36. response to hydrogen peroxide Source: BHF-UCL
  37. response to lipid hydroperoxide Source: Ensembl
  38. response to nicotine Source: Ensembl
  39. response to selenium ion Source: BHF-UCL
  40. response to symbiotic bacterium Source: Ensembl
  41. response to toxic substance Source: Ensembl
  42. response to xenobiotic stimulus Source: Ensembl
  43. sensory perception of sound Source: Ensembl
  44. skeletal muscle fiber development Source: Ensembl
  45. skeletal muscle tissue regeneration Source: Ensembl
  46. small molecule metabolic process Source: Reactome
  47. temperature homeostasis Source: Ensembl
  48. triglyceride metabolic process Source: Ensembl
  49. UV protection Source: BHF-UCL
  50. vasodilation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciMetaCyc:HS00019-MONOMER.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150209. Synthesis of 5-eicosatetraenoic acids.
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_172715. Detoxification of Reactive Oxygen Species.
REACT_2086. Purine catabolism.

Protein family/group databases

PeroxiBasei3600. HsGPx01-A.

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
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:4553. GPX1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. mitochondrial matrix Source: Reactome
  5. mitochondrion Source: BHF-UCL
  6. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

MIMi138320. gene+phenotype.
PharmGKBiPA28949.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Glutathione peroxidase 1PRO_0000066610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881N6-acetyllysine; alternateBy similarity
Modified residuei88 – 881N6-succinyllysine; alternateBy similarity
Modified residuei114 – 1141N6-acetyllysine; alternateBy similarity
Modified residuei114 – 1141N6-succinyllysine; alternateBy similarity
Modified residuei148 – 1481N6-acetyllysine; alternateBy similarity
Modified residuei148 – 1481N6-succinyllysine; alternateBy similarity

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

Proteomic databases

MaxQBiP07203.
PaxDbiP07203.
PRIDEiP07203.

2D gel databases

OGPiP07203.
SWISS-2DPAGEP07203.

PTM databases

PhosphoSiteiP07203.

Expressioni

Gene expression databases

BgeeiP07203.
CleanExiHS_GPX1.
ExpressionAtlasiP07203. baseline.
GenevestigatoriP07203.

Organism-specific databases

HPAiCAB011582.
HPA044758.

Interactioni

Subunit structurei

Homotetramer. Interacts with MIEN1.

Protein-protein interaction databases

BioGridi109134. 8 interactions.
IntActiP07203. 1 interaction.
STRINGi9606.ENSP00000407375.

Structurei

Secondary structure

1
203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 183
Helixi32 – 354
Beta strandi38 – 458
Beta strandi47 – 493
Helixi52 – 6615
Helixi67 – 693
Beta strandi71 – 777
Turni82 – 854
Helixi89 – 913
Helixi92 – 987
Beta strandi108 – 1125
Helixi124 – 1329
Helixi147 – 1493
Beta strandi152 – 1543
Beta strandi166 – 1694
Beta strandi175 – 1795
Helixi185 – 1884
Helixi189 – 1968

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F8AX-ray1.50A/B14-198[»]
ProteinModelPortaliP07203.
SMRiP07203. Positions 14-197.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07203.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP07203.
KOiK00432.
OMAiGHQENTK.
OrthoDBiEOG7KQ23C.
PhylomeDBiP07203.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931L → Q in CAA31992. (PubMed:2955287)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51R → P.1 Publication
Corresponds to variant rs8179169 [ dbSNP | Ensembl ].
VAR_020912
Natural varianti7 – 82Missing.5 Publications
VAR_020913
Natural varianti8 – 81Missing.3 Publications
VAR_020914
Natural varianti194 – 1941A → T.1 Publication
Corresponds to variant rs6446261 [ dbSNP | Ensembl ].
VAR_020915
Natural varianti200 – 2001P → L Frequent polymorphism. 4 Publications
Corresponds to variant rs1050450 [ dbSNP | Ensembl ].
VAR_007904

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei85 – 9814ENAKN…NSLKY → VRRAERGGAGADVQ in isoform 2. CuratedVSP_047369Add
BLAST
Alternative sequencei99 – 203105Missing in isoform 2. CuratedVSP_047370Add
BLAST

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei49 – 491Selenocysteine

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_000581.2. [P07203-1]
NP_958799.1. NM_201397.1. [P07203-2]
UniGeneiHs.76686.

Genome annotation databases

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

Polymorphism databases

DMDMi311033481.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Selenocysteine

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Glutathione peroxidase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS43091.1. [P07203-1 ]
CCDS54582.1. [P07203-2 ]
PIRi A42152. OPHUE.
RefSeqi NP_000572.2. NM_000581.2. [P07203-1 ]
NP_958799.1. NM_201397.1. [P07203-2 ]
UniGenei Hs.76686.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2F8A X-ray 1.50 A/B 14-198 [» ]
ProteinModelPortali P07203.
SMRi P07203. Positions 14-197.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109134. 8 interactions.
IntActi P07203. 1 interaction.
STRINGi 9606.ENSP00000407375.

Chemistry

ChEMBLi CHEMBL2163186.
DrugBanki DB00143. Glutathione.

Protein family/group databases

PeroxiBasei 3600. HsGPx01-A.

PTM databases

PhosphoSitei P07203.

Polymorphism databases

DMDMi 311033481.

2D gel databases

OGPi P07203.
SWISS-2DPAGE P07203.

Proteomic databases

MaxQBi P07203.
PaxDbi P07203.
PRIDEi P07203.

Protocols and materials databases

DNASUi 2876.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000419349 ; ENSP00000391316 ; ENSG00000233276 . [P07203-2 ]
ENST00000419783 ; ENSP00000407375 ; ENSG00000233276 . [P07203-1 ]
GeneIDi 2876.
KEGGi hsa:2876.
UCSCi uc021wxw.1. human. [P07203-1 ]

Organism-specific databases

CTDi 2876.
GeneCardsi GC03M049369.
H-InvDB HIX0003298.
HGNCi HGNC:4553. GPX1.
HPAi CAB011582.
HPA044758.
MIMi 138320. gene+phenotype.
neXtProti NX_P07203.
PharmGKBi PA28949.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0386.
GeneTreei ENSGT00760000119230.
HOGENOMi HOG000277055.
HOVERGENi HBG004333.
InParanoidi P07203.
KOi K00432.
OMAi GHQENTK.
OrthoDBi EOG7KQ23C.
PhylomeDBi P07203.
TreeFami TF105318.

Enzyme and pathway databases

BioCyci MetaCyc:HS00019-MONOMER.
Reactomei REACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150209. Synthesis of 5-eicosatetraenoic acids.
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_172715. Detoxification of Reactive Oxygen Species.
REACT_2086. Purine catabolism.

Miscellaneous databases

ChiTaRSi GPX1. human.
EvolutionaryTracei P07203.
GeneWikii GPX1.
GenomeRNAii 2876.
NextBioi 11353.
PROi P07203.
SOURCEi Search...

Gene expression databases

Bgeei P07203.
CleanExi HS_GPX1.
ExpressionAtlasi P07203. baseline.
Genevestigatori P07203.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
PANTHERi PTHR11592. PTHR11592. 1 hit.
Pfami PF00255. GSHPx. 1 hit.
[Graphical view ]
PIRSFi PIRSF000303. Glutathion_perox. 1 hit.
PRINTSi PR01011. GLUTPROXDASE.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence coding for human glutathione peroxidase."
    Sukenaga Y., Ishida K., Takeda T., Takagi K.
    Nucleic Acids Res. 15:7178-7178(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 7-ALA-ALA-8 DEL.
  2. "Nucleotide sequence of a human gene for glutathione peroxidase."
    Ishida K., Morino T., Takagi K., Sukenaga Y.
    Nucleic Acids Res. 15:10051-10051(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT 7-ALA-ALA-8 DEL.
  3. "Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine."
    Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Hallewell R.A.
    Nucleic Acids Res. 15:5484-5484(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 7-ALA-ALA-8 DEL.
    Tissue: Kidney.
  4. "Isolation and chromosomal localization of the human glutathione peroxidase gene."
    Chada S., le Beau M.M., Casey L., Newburger P.E.
    Genomics 6:268-271(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 7-ALA-ALA-8 DEL.
  5. "Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1)."
    Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.
    J. Biol. Chem. 267:5949-5958(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ALA-8 DEL.
  6. NIEHS SNPs program
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS PRO-5; THR-194 AND LEU-200.
  7. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of the selenocysteine to glycine mutant of human glutathione peroxidase 1."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 14-198.
  11. "Low yield of polymorphisms from EST blast searching: analysis of genes related to oxidative stress and verification of the P197L polymorphism in GPX1."
    Forsberg L., de Faire U., Morgenstern R.
    Hum. Mutat. 13:294-300(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-200.
  12. "Association between the GCG polymorphism of the selenium dependent GPX1 gene and the risk of young onset prostate cancer."
    Kote-Jarai Z., Durocher F., Edwards S.M., Hamoudi R., Jackson R.A., Ardern-Jones A., Murkin A., Dearnaley D.P., Kirby R., Houlston R., Easton D.F., Eeles R.
    Prostate Cancer Prostatic Dis. 5:189-192(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ALA-8 DEL AND 7-ALA-ALA-8 DEL.
  13. "Functional variants in the glutathione peroxidase-1 (GPx-1) gene are associated with increased intima-media thickness of carotid arteries and risk of macrovascular diseases in Japanese type 2 diabetic patients."
    Hamanishi T., Furuta H., Kato H., Doi A., Tamai M., Shimomura H., Sakagashira S., Nishi M., Sasaki H., Sanke T., Nanjo K.
    Diabetes 53:2455-2460(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ALA-8 DEL AND LEU-200.
  14. "Increased risk of bladder cancer associated with a glutathione peroxidase 1 codon 198 variant."
    Ichimura Y., Habuchi T., Tsuchiya N., Wang L., Oyama C., Sato K., Nishiyama H., Ogawa O., Kato T.
    J. Urol. 172:728-732(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-200.

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: October 29, 2014
This is version 173 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

External Data

Dasty 3