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UniProtKB/Swiss-Prot entry P07203


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPX1_HUMAN
Primary accession number P07203
Secondary accession numbers Q7Z5H1 Q9BW12
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on February 26, 2008 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 108)
Name and origin of the protein
Protein name Glutathione peroxidase 1
Synonyms EC 1.11.1.9
GSHPx-1
GPx-1
Cellular glutathione peroxidase
Gene name
Name: GPX1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/15.17.7178; PubMed=3658677 [NCBI, ExPASy, EBI, Israel, Japan]
Sukenaga Y., Ishida K., Takeda T., Takagi K.;
"cDNA sequence coding for human glutathione peroxidase.";
Nucleic Acids Res. 15:7178-7178(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/15.23.10051; PubMed=3697069 [NCBI, ExPASy, EBI, Israel, Japan]
Ishida K., Morino T., Takagi K., Sukenaga Y.;
"Nucleotide sequence of a human gene for glutathione peroxidase.";
Nucleic Acids Res. 15:10051-10051(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
DOI=10.1093/nar/15.13.5484; PubMed=2955287 [NCBI, ExPASy, EBI, Israel, Japan]
Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Hallewell R.A.;
"Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine.";
Nucleic Acids Res. 15:5484-5484(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0888-7543(90)90566-D; PubMed=2307470 [NCBI, ExPASy, EBI, Israel, Japan]
Chada S., le Beau M.M., Casey L., Newburger P.E.;
"Isolation and chromosomal localization of the human glutathione peroxidase gene.";
Genomics 6:268-271(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-11 INS.
PubMed=1556108 [NCBI, ExPASy, EBI, Israel, Japan]
Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.;
"Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1).";
J. Biol. Chem. 267:5949-5958(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-5; ALA-ALA-11 INS; THR-192 AND LEU-198.
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
VARIANT LEU-198.
DOI=10.1002/(SICI)1098-1004(1999)13:4<294::AID-HUMU6>3.0.CO;2-5; PubMed=10220143 [NCBI, ExPASy, EBI, Israel, Japan]
Forsberg L., de Faire U., Morgenstern R.;
"Low yield of polymorphisms from EST blast searching: analysis of genes related to oxidative stress and verification of the P197L polymorphism in GPX1.";
Hum. Mutat. 13:294-300(1999).
[9]
VARIANTS ALA-11 INS AND ALA-ALA-11 INS.
DOI=10.1038/sj.pcan.4500569; PubMed=12496980 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Association between the GCG polymorphism of the selenium dependent GPX1 gene and the risk of young onset prostate cancer.";
Prostate Cancer Prostatic Dis. 5:189-192(2002).
[10]
VARIANTS ALA-11 INS AND LEU-198.
PubMed=15331559 [NCBI, ExPASy, EBI, Israel, Japan]
Hamanishi T., Furuta H., Kato H., Doi A., Tamai M., Shimomura H., Sakagashira S., Nishi M., Sasaki H., Sanke T., Nanjo K.;
"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.";
Diabetes 53:2455-2460(2004).
[11]
VARIANT LEU-198.
DOI=10.1097/01.ju.0000130942.40597.9d; PubMed=15247771 [NCBI, ExPASy, EBI, Israel, Japan]
Ichimura Y., Habuchi T., Tsuchiya N., Wang L., Oyama C., Sato K., Nishiyama H., Ogawa O., Kato T.;
"Increased risk of bladder cancer associated with a glutathione peroxidase 1 codon 198 variant.";
J. Urol. 172:728-732(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00433; CAA68491.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00483; CAB37833.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13709; CAA31992.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13710; CAA31993.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21304; AAA75389.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M83094; AAA67540.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY327818; AAP80181.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000742; AAH00742.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A42152; OPHUE.
RefSeq NP_000572.2; -.
NP_958799.1; -.
UniGene Hs.76686
3D structure databases
PDB
2F8A; X-ray; 1.50 A; A/B=12-196.[ExPASy / RCSB / EBI]
PDBsum 2F8A; -.
ModBase P07203.
Protein family/group databases
PeroxiBase 3600; HsGPx01-a.
PTM databases
PhosphoSite P07203; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-9882; -.
Polymorphism databases
NIEHS-SNPs GPX1.
2D gel databases
SWISS-2DPAGE P07203; -.
OGP P07203; -.
Organism-specific databases
H-InvDB HIX0003298; -.
HGNC HGNC:4553; GPX1.
GenAtlas GPX1.
MIM 138320; gene+phenotype. [NCBI / EBI]
Orphanet 98363; Anaemia, haemolytic.
PharmGKB PA28949; -.
GeneCards P07203.
Gene expression databases
CleanEx HS_GPX1; -.
GermOnline ENSG00000211447; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0043295; Molecular function: glutathione binding (inferred by curator from UniProtKB).
GO:0004602; Molecular function: glutathione peroxidase activity (inferred from direct assay from UniProtKB).
GO:0008539; Molecular function: proteasome inhibitor activity (inferred from direct assay from UniProtKB).
GO:0017124; Molecular function: SH3 domain binding (inferred from physical interaction from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0006749; Biological process: glutathione metabolic process (inferred from direct assay from UniProtKB).
GO:0060047; Biological process: heart contraction (inferred from mutant phenotype from UniProtKB).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from direct assay from UniProtKB).
GO:0043154; Biological process: negative regulation of caspase activity (inferred from mutant phenotype from UniProtKB).
GO:0040029; Biological process: regulation of gene expression, epigenetic (inferred from direct assay from UniProtKB).
GO:0033599; Biological process: regulation of mammary gland epithelial cell proliferation (inferred from mutant phenotype from UniProtKB).
GO:0001836; Biological process: release of cytochrome c from mitochondria (inferred from mutant phenotype from UniProtKB).
GO:0010269; Biological process: response to selenium ion (inferred from mutant phenotype from UniProtKB).
GO:0009650; Biological process: UV protection (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000889; Glut_peroxidase.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
PANTHER PTHR11592; Glut_peroxidase; 1.
Pfam PF00255; GSHPx; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000303; Glutathion_perox; 1.
PRINTS PR01011; GLUTPROXDASE.
PROSITE PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P07203.
ProtoNet P07203.
Genome annotation databases
Ensembl ENSG00000197582; Homo sapiens. [Contig view]
GeneID 2876; -.
KEGG hsa:2876; -.
son:SO_1799; -.
Phylogenomic databases
HOGENOM P07203; -.
HOVERGEN P07203; -.
Other
DrugBank DB00143; Glutathione.
LinkHub P07203; -.
NextBio 11353; -.
SOURCE GPX1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Oxidoreductase; Peroxidase; Polymorphism; Selenium; Selenocysteine.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   201  201     Glutathione peroxidase 1. PRO_0000066610
ACT_SITE   47    47         
NON_STD   47    47        Selenocysteine. 
MOD_RES   146   146        N6-acetyllysine (By similarity). 
VARIANT   5     5  1     R -> P. VAR_020912 
VARIANT   11    11  1     A -> AA. VAR_020913
VARIANT   11    11  1     A -> AAA. VAR_020914
VARIANT   192   192  1     A -> T. VAR_020915 
VARIANT   198   198  1     P -> L (in 30% of the population; associated with an increased risk of cancer; dbSNP:rs1050450 [NCBI]). VAR_007904 
CONFLICT   91    91        L -> Q (in Ref. 3; CAA31992). 
HELIX   14    16  3      
HELIX   30    33  4      
STRAND   36    43  8      
STRAND   45    47  3      
HELIX   50    64  15      
HELIX   65    67  3      
STRAND   69    75  7      
TURN   80    83  4      
HELIX   87    89  3      
HELIX   90    96  7      
STRAND   106   110  5      
HELIX   122   130  9      
STRAND   138   144  7      
HELIX   145   147  3      
STRAND   150   154  5      
STRAND   164   167  4      
STRAND   173   177  5      
HELIX   183   186  4      
HELIX   187   194  8      
Sequence information
Length: 201 AA [This is the length of the unprocessed precursor] Molecular weight: 21946 Da [This is the MW of the unprocessed precursor] CRC64: E84C559299F9811E [This is a checksum on the sequence]
        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 

P07203 in FASTA format

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