Glutathione peroxidase 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P07203 (GPX1_HUMAN)

Last modified June 16, 2009. Version 116. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Glutathione peroxidase 1
    EC=1.11.1.9
Alternative name(s):
    GSHPx-1
      Short name=GPx-1
    Cellular glutathione peroxidase

Gene names

Name:

GPX1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Protects the hemoglobin in erythrocytes from oxidative breakdown.
Catalytic activity	2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glutathione peroxidase family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism Selenocysteine
Ligand	Selenium
Molecular function	Oxidoreductase Peroxidase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	UV protection Inferred from mutant phenotype. Source: UniProtKB anti-apoptosis Inferred from mutant phenotype. Source: UniProtKB glutathione metabolic process Inferred from direct assay. Source: UniProtKB heart contraction Inferred from mutant phenotype. Source: UniProtKB hydrogen peroxide catabolic process Inferred from direct assay. Source: UniProtKB negative regulation of caspase activity Inferred from mutant phenotype. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of gene expression, epigenetic Inferred from direct assay. Source: UniProtKB regulation of mammary gland epithelial cell proliferation Inferred from mutant phenotype. Source: UniProtKB release of cytochrome c from mitochondria Inferred from mutant phenotype. Source: UniProtKB response to selenium ion Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome mitochondrion Inferred from direct assay. Source: UniProtKB
Molecular function	SH3 domain binding Inferred from physical interaction. Source: UniProtKB glutathione binding Inferred by curator. Source: UniProtKB glutathione peroxidase activity Inferred from direct assay. Source: UniProtKB proteasome inhibitor activity Inferred from direct assay. Source: UniProtKB selenium binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 201

201

Glutathione peroxidase 1

PRO_0000066610

Sites

Active site

Amino acid modifications

Non-standard residue

Selenocysteine

Modified residue

146

N6-acetyllysine By similarity

Natural variations

Natural variant

R → P: dbSNP rs8179169.

VAR_020912

Natural variant

A → AA Ref.5 Ref.11 Ref.12

VAR_020913

Natural variant

A → AAA Ref.5 Ref.11 Ref.12

VAR_020914

Natural variant

192

A → T Ref.6

VAR_020915

Natural variant

198

P → L in 30% of the population; associated with an increased risk of cancer. dbSNP rs1050450. Ref.6 Ref.12 Ref.10 Ref.13

VAR_007904

Experimental info

Sequence conflict

L → Q in CAA31992. Ref.3

Secondary structure

201

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P07203-1 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: E84C559299F9811E
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FASTA

201

21,946

        10         20         30         40         50         60 
MCAARLAAAA AQSVYAFSAR PLAGGEPVSL GSLRGKVLLI ENVASLUGTT VRDYTQMNEL 

        70         80         90        100        110        120 
QRRLGPRGLV VLGFPCNQFG HQENAKNEEI LNSLKYVRPG GGFEPNFMLF EKCEVNGAGA 

       130        140        150        160        170        180 
HPLFAFLREA LPAPSDDATA LMTDPKLITW SPVCRNDVAW NFEKFLVGPD GVPLRRYSRR 

       190        200 
FQTIDIEPDI EALLSQGPSC A

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA sequence coding for human glutathione peroxidase." Sukenaga Y., Ishida K., Takeda T., Takagi K. Nucleic Acids Res. 15:7178-7178(1987) [PubMed: 3658677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 3697069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 2955287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 2307470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 1556108] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-11 INS.
[6]	NIEHS SNPs program Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-5; ALA-ALA-11 INS; THR-192 AND LEU-198.
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"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 12-196.
[10]	"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: 10220143] [Abstract] Cited for: VARIANT LEU-198.
[11]	"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: 12496980] [Abstract] Cited for: VARIANTS ALA-11 INS AND ALA-ALA-11 INS.
[12]	"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: 15331559] [Abstract] Cited for: VARIANTS ALA-11 INS AND LEU-198.
[13]	"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: 15247771] [Abstract] Cited for: VARIANT LEU-198.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

Wikipedia

Glutathione peroxidase entry

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Cross-references

Sequence databases

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.
BC000742 mRNA. Translation: AAH00742.3.

IPI

IPI00927606.

PIR

OPHUE. A42152.

RefSeq

NP_000572.2.
NP_958799.1.

UniGene

Hs.76686

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F8A	X-ray	1.50	A/B	12-196	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

3600. HsGPx01-a.

PTM databases

PhosphoSite

P07203.

2-D gel databases

SWISS-2DPAGE

P07203.

OGP

P07203.

Proteomic databases

PRIDE

P07203.

Genome annotation databases

Ensembl

ENSG00000197582. Homo sapiens. [Contig view]

GeneID

2876.

KEGG

hsa:2876.

Organism-specific databases

GeneCards

GC03M049369.

H-InvDB

HIX0003298.

HGNC

HGNC:4553. GPX1.

MIM

138320. gene+phenotype.

Orphanet

98363. Hemolytic anemia.

PharmGKB

PA28949.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P07203.

HOVERGEN

P07203.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-9882.

BRENDA

1.11.1.9. 247.

Gene expression databases

CleanEx

HS_GPX1.

GermOnline

ENSG00000211447. Homo sapiens.

Family and domain databases

InterPro

IPR000889. Glutathione_peroxidase.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR11592. Glut_peroxidase. 1 hit.

Pfam

PF00255. GSHPx. 1 hit.
[Graphical view]

PIRSF

PIRSF000303. Glutathion_perox. 1 hit.

PRINTS

PR01011. GLUTPROXDASE.

PROSITE

PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

11353.

SOURCE

Search...

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Entry information

Entry name

GPX1_HUMAN

Accession

Primary (citable) accession number: P07203
Secondary accession number(s): Q7Z5H1, Q9BW12

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 26, 2008
Last modified:	June 16, 2009
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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