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P18283

- GPX2_HUMAN

UniProt

P18283 - GPX2_HUMAN

Protein

Glutathione peroxidase 2

Gene

GPX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (26 Feb 2008)
      Previous versions | rss
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    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 oxidative stress Source: InterPro
    4. response to symbiotic bacterium Source: Ensembl
    5. temperature homeostasis Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS11006-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.
    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: 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: UniProt

    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

    ArrayExpressiP18283.
    BgeeiP18283.
    CleanExiHS_GPX2.
    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 – 103
    Beta strandi12 – 154
    Beta strandi20 – 223
    Helixi23 – 264
    Beta strandi29 – 368
    Helixi43 – 5614
    Turni58 – 603
    Beta strandi61 – 688
    Helixi79 – 813
    Helixi82 – 887
    Beta strandi98 – 1025
    Beta strandi105 – 1095
    Helixi114 – 1229
    Helixi137 – 1393
    Beta strandi156 – 1594
    Beta strandi165 – 1695
    Helixi175 – 1784
    Helixi179 – 1868

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000277055.
    HOVERGENiHBG004333.
    InParanoidiP18283.
    KOiK00432.
    OMAiKMVENEY.
    PhylomeDBiP18283.
    TreeFamiTF105318.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR000889. Glutathione_peroxidase.
    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

    MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLU GTTTRDFTQL    50
    NELQCRFPRR LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT 100
    LVQKCEVNGQ NEHPVFAYLK DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV 150
    AWNFEKFLIG PEGEPFRRYS RTFPTINIEP DIKRLLKVAI 190
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS41964.1.
    PIRi A45207.
    RefSeqi NP_002074.2. NM_002083.3.
    UniGenei Hs.2704.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HE3 X-ray 2.10 A 4-188 [» ]
    ProteinModelPortali P18283.
    SMRi P18283. Positions 4-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109135. 3 interactions.
    IntActi P18283. 3 interactions.
    STRINGi 9606.ENSP00000374265.

    Chemistry

    DrugBanki DB00143. Glutathione.

    Protein family/group databases

    PeroxiBasei 3601. HsGPx02.

    PTM databases

    PhosphoSitei P18283.

    Polymorphism databases

    DMDMi 172046064.

    Proteomic databases

    MaxQBi P18283.
    PaxDbi P18283.
    PRIDEi P18283.

    Protocols and materials databases

    DNASUi 2877.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389614 ; ENSP00000374265 ; ENSG00000176153 .
    GeneIDi 2877.
    KEGGi hsa:2877.
    UCSCi uc021ruq.2. human.

    Organism-specific databases

    CTDi 2877.
    GeneCardsi GC14M065405.
    H-InvDB HIX0037716.
    HGNCi HGNC:4554. GPX2.
    HPAi HPA003545.
    MIMi 138319. gene.
    neXtProti NX_P18283.
    PharmGKBi PA28950.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0386.
    HOGENOMi HOG000277055.
    HOVERGENi HBG004333.
    InParanoidi P18283.
    KOi K00432.
    OMAi KMVENEY.
    PhylomeDBi P18283.
    TreeFami TF105318.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS11006-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.
    SABIO-RK P18283.

    Miscellaneous databases

    EvolutionaryTracei P18283.
    GeneWikii GPX2_(gene).
    GenomeRNAii 2877.
    NextBioi 11359.
    PROi P18283.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18283.
    Bgeei P18283.
    CleanExi HS_GPX2.
    Genevestigatori P18283.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR000889. Glutathione_peroxidase.
    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

    1. "A human cDNA sequence of a novel glutathione peroxidase-related protein."
      Akasaka M., Mizoguchi J., Takahashi K.
      Nucleic Acids Res. 18:4619-4619(1990) [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(1993) [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(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-37.
    4. NIEHS SNPs program
      Submitted (OCT-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(2003) [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(2004) [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 (FEB-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: October 1, 2014
    This is version 143 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