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P09211

- GSTP1_HUMAN

UniProt

P09211 - GSTP1_HUMAN

Protein

Glutathione S-transferase P

Gene

GSTP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.1 Publication

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei8 – 81Glutathione1 Publication
    Binding sitei14 – 141Glutathione1 Publication
    Binding sitei39 – 391Glutathione1 Publication
    Binding sitei45 – 451GlutathioneBy similarity

    GO - Molecular functioni

    1. dinitrosyl-iron complex binding Source: BHF-UCL
    2. glutathione transferase activity Source: UniProtKB
    3. JUN kinase binding Source: BHF-UCL
    4. kinase regulator activity Source: BHF-UCL
    5. nitric oxide binding Source: BHF-UCL
    6. protein binding Source: IntAct
    7. S-nitrosoglutathione binding Source: BHF-UCL

    GO - Biological processi

    1. cellular response to lipopolysaccharide Source: BHF-UCL
    2. central nervous system development Source: ProtInc
    3. common myeloid progenitor cell proliferation Source: BHF-UCL
    4. glutathione derivative biosynthetic process Source: Reactome
    5. glutathione metabolic process Source: UniProtKB
    6. negative regulation of acute inflammatory response Source: BHF-UCL
    7. negative regulation of apoptotic process Source: UniProtKB
    8. negative regulation of biosynthetic process Source: BHF-UCL
    9. negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    10. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    11. negative regulation of fibroblast proliferation Source: BHF-UCL
    12. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
    13. negative regulation of interleukin-1 beta production Source: BHF-UCL
    14. negative regulation of JUN kinase activity Source: BHF-UCL
    15. negative regulation of leukocyte proliferation Source: BHF-UCL
    16. negative regulation of MAPK cascade Source: BHF-UCL
    17. negative regulation of MAP kinase activity Source: BHF-UCL
    18. negative regulation of monocyte chemotactic protein-1 production Source: BHF-UCL
    19. negative regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
    20. negative regulation of protein kinase activity Source: BHF-UCL
    21. negative regulation of stress-activated MAPK cascade Source: BHF-UCL
    22. negative regulation of tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
    23. negative regulation of tumor necrosis factor production Source: BHF-UCL
    24. nitric oxide storage Source: BHF-UCL
    25. positive regulation of superoxide anion generation Source: BHF-UCL
    26. regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    27. regulation of stress-activated MAPK cascade Source: BHF-UCL
    28. response to reactive oxygen species Source: BHF-UCL
    29. small molecule metabolic process Source: Reactome
    30. xenobiotic metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_6926. Glutathione conjugation.
    SABIO-RKP09211.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase P (EC:2.5.1.18)
    Alternative name(s):
    GST class-pi
    GSTP1-1
    Gene namesi
    Name:GSTP1
    Synonyms:FAEES3, GST3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:4638. GSTP1.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion 1 Publication. Nucleus 1 Publication
    Note: The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. intracellular Source: BHF-UCL
    6. mitochondrion Source: HPA
    7. nucleus Source: UniProtKB-SubCell
    8. plasma membrane Source: HPA
    9. TRAF2-GSTP1 complex Source: BHF-UCL
    10. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi8 – 81Y → F: Reduces catalytic activity about 50-fold. 2 Publications
    Mutagenesisi99 – 991D → A: Reduces affinity for glutathione. Slightly reduced catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA29028.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 210209Glutathione S-transferase PPRO_0000185900Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41Phosphotyrosine; by EGFR1 Publication
    Modified residuei103 – 1031N6-succinyllysineBy similarity
    Modified residuei116 – 1161N6-succinyllysineBy similarity
    Modified residuei128 – 1281N6-acetyllysine1 Publication
    Modified residuei199 – 1991Phosphotyrosine; by EGFR1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP09211.
    PaxDbiP09211.
    PRIDEiP09211.

    2D gel databases

    DOSAC-COBS-2DPAGEP09211.
    OGPiP09211.
    REPRODUCTION-2DPAGEIPI00219757.
    SWISS-2DPAGEP09211.
    UCD-2DPAGEP09211.

    PTM databases

    PhosphoSiteiP09211.

    Miscellaneous databases

    PMAP-CutDBP09211.

    Expressioni

    Gene expression databases

    ArrayExpressiP09211.
    BgeeiP09211.
    CleanExiHS_GSTP1.
    GenevestigatoriP09211.

    Organism-specific databases

    HPAiCAB019298.
    HPA019779.
    HPA019869.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CDK5.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRDX6P300412EBI-353467,EBI-2255129
    TRAF2Q129335EBI-353467,EBI-355744

    Protein-protein interaction databases

    BioGridi109205. 27 interactions.
    IntActiP09211. 25 interactions.
    MINTiMINT-4998983.
    STRINGi9606.ENSP00000381607.

    Structurei

    Secondary structure

    1
    210
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Beta strandi10 – 123
    Helixi13 – 153
    Helixi16 – 249
    Beta strandi29 – 335
    Helixi36 – 416
    Helixi43 – 475
    Beta strandi48 – 514
    Beta strandi55 – 584
    Beta strandi61 – 644
    Helixi66 – 7611
    Helixi84 – 11027
    Helixi112 – 13524
    Helixi138 – 1403
    Beta strandi144 – 1485
    Helixi151 – 16616
    Helixi170 – 1734
    Helixi175 – 18511
    Helixi188 – 1958
    Helixi197 – 2004
    Beta strandi204 – 2085

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    10GSX-ray2.20A/B2-210[»]
    11GSX-ray2.30A/B1-210[»]
    12GSX-ray2.10A/B1-210[»]
    13GSX-ray1.90A/B1-210[»]
    14GSX-ray2.80A/B1-210[»]
    16GSX-ray1.90A/B1-210[»]
    17GSX-ray1.90A/B1-210[»]
    18GSX-ray1.90A/B1-210[»]
    19GSX-ray1.90A/B2-210[»]
    1AQVX-ray1.94A/B2-210[»]
    1AQWX-ray1.80A/B/C/D2-210[»]
    1AQXX-ray2.00A/B/C/D2-210[»]
    1EOGX-ray2.10A/B3-210[»]
    1EOHX-ray2.50A/B/C/D/E/F/G/H2-210[»]
    1GSSX-ray2.80A/B2-210[»]
    1KBNX-ray2.00A/B2-210[»]
    1LBKX-ray1.86A/B2-203[»]
    1MD3X-ray2.03A/B2-210[»]
    1MD4X-ray2.10A/B2-210[»]
    1PGTX-ray1.80A/B1-210[»]
    1PX6X-ray2.10A/B2-210[»]
    1PX7X-ray2.03A/B2-210[»]
    1ZGNX-ray2.10A/B2-210[»]
    20GSX-ray2.45A/B2-210[»]
    22GSX-ray1.90A/B1-210[»]
    2A2RX-ray1.40A/B1-210[»]
    2A2SX-ray1.70A/B1-210[»]
    2GSSX-ray1.90A/B2-210[»]
    2J9HX-ray2.40A/B2-210[»]
    2PGTX-ray1.90A/B1-210[»]
    3CSHX-ray1.55A/B2-210[»]
    3CSIX-ray1.90A/B/C/D2-210[»]
    3CSJX-ray1.90A/B2-210[»]
    3DD3X-ray2.25A/B1-210[»]
    3DGQX-ray1.60A/B1-210[»]
    3GSSX-ray1.90A/B2-210[»]
    3GUSX-ray1.53A/B2-210[»]
    3HJMX-ray2.10A/B/C/D2-210[»]
    3HJOX-ray1.95A/B2-210[»]
    3HKRX-ray1.80A/B2-210[»]
    3IE3X-ray1.80A/B2-210[»]
    3KM6X-ray2.10A/B2-210[»]
    3KMNX-ray1.80A/B2-210[»]
    3KMOX-ray2.60A/B2-210[»]
    3N9JX-ray1.85A/B1-210[»]
    3PGTX-ray2.14A/B1-210[»]
    4GSSX-ray2.50A/B2-210[»]
    4PGTX-ray2.10A/B1-210[»]
    5GSSX-ray1.95A/B2-210[»]
    6GSSX-ray1.90A/B2-210[»]
    7GSSX-ray2.20A/B2-210[»]
    8GSSX-ray1.90A/B/C2-210[»]
    9GSSX-ray1.97A/B2-210[»]
    ProteinModelPortaliP09211.
    SMRiP09211. Positions 1-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09211.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8180GST N-terminalAdd
    BLAST
    Domaini83 – 204122GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 532Glutathione binding
    Regioni65 – 662Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Pi family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiKOG1695.
    HOGENOMiHOG000115733.
    HOVERGENiHBG108324.
    InParanoidiP09211.
    KOiK00799.
    OMAiANSIYIV.
    OrthoDBiEOG7KH9M3.
    PhylomeDBiP09211.
    TreeFamiTF105321.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR003082. GST_pi.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01268. GSTRNSFRASEP.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P09211-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPYTVVYFP VRGRCAALRM LLADQGQSWK EEVVTVETWQ EGSLKASCLY    50
    GQLPKFQDGD LTLYQSNTIL RHLGRTLGLY GKDQQEAALV DMVNDGVEDL 100
    RCKYISLIYT NYEAGKDDYV KALPGQLKPF ETLLSQNQGG KTFIVGDQIS 150
    FADYNLLDLL LIHEVLAPGC LDAFPLLSAY VGRLSARPKL KAFLASPEYV 200
    NLPINGNGKQ 210
    Length:210
    Mass (Da):23,356
    Last modified:January 23, 2007 - v2
    Checksum:i409E33FFAA338396
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1861A → P in CAA30894. (PubMed:3196325)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051I → V in allele GSTP1*B and allele GSTP1*C. 3 Publications
    Corresponds to variant rs1695 [ dbSNP | Ensembl ].
    VAR_014499
    Natural varianti114 – 1141A → V in allele GSTP1*C. 2 Publications
    Corresponds to variant rs1138272 [ dbSNP | Ensembl ].
    VAR_014500
    Natural varianti169 – 1691G → D.
    Corresponds to variant rs41462048 [ dbSNP | Ensembl ].
    VAR_049493

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06547 mRNA. Translation: CAA29794.1.
    M24485 Genomic DNA. Translation: AAA56823.1.
    X08058 Genomic DNA. Translation: CAA30847.1.
    X08094, X08095, X08096 Genomic DNA. Translation: CAA30894.1.
    X15480 mRNA. Translation: CAA33508.1.
    U12472 Genomic DNA. Translation: AAA64919.1.
    U30897 mRNA. Translation: AAC51280.1.
    U62589 mRNA. Translation: AAC51237.1.
    U21689 Genomic DNA. Translation: AAC13869.1.
    BT019949 mRNA. Translation: AAV38752.1.
    BT019950 mRNA. Translation: AAV38753.1.
    CR450361 mRNA. Translation: CAG29357.1.
    AY324387 Genomic DNA. Translation: AAP72967.1.
    BC010915 mRNA. Translation: AAH10915.1.
    CCDSiCCDS41679.1.
    PIRiA41177.
    JS0153. A37378.
    RefSeqiNP_000843.1. NM_000852.3.
    UniGeneiHs.523836.

    Genome annotation databases

    EnsembliENST00000398606; ENSP00000381607; ENSG00000084207.
    GeneIDi2950.
    KEGGihsa:2950.
    UCSCiuc001omf.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06547 mRNA. Translation: CAA29794.1 .
    M24485 Genomic DNA. Translation: AAA56823.1 .
    X08058 Genomic DNA. Translation: CAA30847.1 .
    X08094 , X08095 , X08096 Genomic DNA. Translation: CAA30894.1 .
    X15480 mRNA. Translation: CAA33508.1 .
    U12472 Genomic DNA. Translation: AAA64919.1 .
    U30897 mRNA. Translation: AAC51280.1 .
    U62589 mRNA. Translation: AAC51237.1 .
    U21689 Genomic DNA. Translation: AAC13869.1 .
    BT019949 mRNA. Translation: AAV38752.1 .
    BT019950 mRNA. Translation: AAV38753.1 .
    CR450361 mRNA. Translation: CAG29357.1 .
    AY324387 Genomic DNA. Translation: AAP72967.1 .
    BC010915 mRNA. Translation: AAH10915.1 .
    CCDSi CCDS41679.1.
    PIRi A41177.
    JS0153. A37378.
    RefSeqi NP_000843.1. NM_000852.3.
    UniGenei Hs.523836.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    10GS X-ray 2.20 A/B 2-210 [» ]
    11GS X-ray 2.30 A/B 1-210 [» ]
    12GS X-ray 2.10 A/B 1-210 [» ]
    13GS X-ray 1.90 A/B 1-210 [» ]
    14GS X-ray 2.80 A/B 1-210 [» ]
    16GS X-ray 1.90 A/B 1-210 [» ]
    17GS X-ray 1.90 A/B 1-210 [» ]
    18GS X-ray 1.90 A/B 1-210 [» ]
    19GS X-ray 1.90 A/B 2-210 [» ]
    1AQV X-ray 1.94 A/B 2-210 [» ]
    1AQW X-ray 1.80 A/B/C/D 2-210 [» ]
    1AQX X-ray 2.00 A/B/C/D 2-210 [» ]
    1EOG X-ray 2.10 A/B 3-210 [» ]
    1EOH X-ray 2.50 A/B/C/D/E/F/G/H 2-210 [» ]
    1GSS X-ray 2.80 A/B 2-210 [» ]
    1KBN X-ray 2.00 A/B 2-210 [» ]
    1LBK X-ray 1.86 A/B 2-203 [» ]
    1MD3 X-ray 2.03 A/B 2-210 [» ]
    1MD4 X-ray 2.10 A/B 2-210 [» ]
    1PGT X-ray 1.80 A/B 1-210 [» ]
    1PX6 X-ray 2.10 A/B 2-210 [» ]
    1PX7 X-ray 2.03 A/B 2-210 [» ]
    1ZGN X-ray 2.10 A/B 2-210 [» ]
    20GS X-ray 2.45 A/B 2-210 [» ]
    22GS X-ray 1.90 A/B 1-210 [» ]
    2A2R X-ray 1.40 A/B 1-210 [» ]
    2A2S X-ray 1.70 A/B 1-210 [» ]
    2GSS X-ray 1.90 A/B 2-210 [» ]
    2J9H X-ray 2.40 A/B 2-210 [» ]
    2PGT X-ray 1.90 A/B 1-210 [» ]
    3CSH X-ray 1.55 A/B 2-210 [» ]
    3CSI X-ray 1.90 A/B/C/D 2-210 [» ]
    3CSJ X-ray 1.90 A/B 2-210 [» ]
    3DD3 X-ray 2.25 A/B 1-210 [» ]
    3DGQ X-ray 1.60 A/B 1-210 [» ]
    3GSS X-ray 1.90 A/B 2-210 [» ]
    3GUS X-ray 1.53 A/B 2-210 [» ]
    3HJM X-ray 2.10 A/B/C/D 2-210 [» ]
    3HJO X-ray 1.95 A/B 2-210 [» ]
    3HKR X-ray 1.80 A/B 2-210 [» ]
    3IE3 X-ray 1.80 A/B 2-210 [» ]
    3KM6 X-ray 2.10 A/B 2-210 [» ]
    3KMN X-ray 1.80 A/B 2-210 [» ]
    3KMO X-ray 2.60 A/B 2-210 [» ]
    3N9J X-ray 1.85 A/B 1-210 [» ]
    3PGT X-ray 2.14 A/B 1-210 [» ]
    4GSS X-ray 2.50 A/B 2-210 [» ]
    4PGT X-ray 2.10 A/B 1-210 [» ]
    5GSS X-ray 1.95 A/B 2-210 [» ]
    6GSS X-ray 1.90 A/B 2-210 [» ]
    7GSS X-ray 2.20 A/B 2-210 [» ]
    8GSS X-ray 1.90 A/B/C 2-210 [» ]
    9GSS X-ray 1.97 A/B 2-210 [» ]
    ProteinModelPortali P09211.
    SMRi P09211. Positions 1-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109205. 27 interactions.
    IntActi P09211. 25 interactions.
    MINTi MINT-4998983.
    STRINGi 9606.ENSP00000381607.

    Chemistry

    BindingDBi P09211.
    ChEMBLi CHEMBL3902.
    DrugBanki DB00903. Ethacrynic acid.
    DB00143. Glutathione.

    PTM databases

    PhosphoSitei P09211.

    2D gel databases

    DOSAC-COBS-2DPAGE P09211.
    OGPi P09211.
    REPRODUCTION-2DPAGE IPI00219757.
    SWISS-2DPAGE P09211.
    UCD-2DPAGE P09211.

    Proteomic databases

    MaxQBi P09211.
    PaxDbi P09211.
    PRIDEi P09211.

    Protocols and materials databases

    DNASUi 2950.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398606 ; ENSP00000381607 ; ENSG00000084207 .
    GeneIDi 2950.
    KEGGi hsa:2950.
    UCSCi uc001omf.3. human.

    Organism-specific databases

    CTDi 2950.
    GeneCardsi GC11P067351.
    HGNCi HGNC:4638. GSTP1.
    HPAi CAB019298.
    HPA019779.
    HPA019869.
    MIMi 134660. gene.
    neXtProti NX_P09211.
    PharmGKBi PA29028.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi KOG1695.
    HOGENOMi HOG000115733.
    HOVERGENi HBG108324.
    InParanoidi P09211.
    KOi K00799.
    OMAi ANSIYIV.
    OrthoDBi EOG7KH9M3.
    PhylomeDBi P09211.
    TreeFami TF105321.

    Enzyme and pathway databases

    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_6926. Glutathione conjugation.
    SABIO-RK P09211.

    Miscellaneous databases

    ChiTaRSi GSTP1. human.
    EvolutionaryTracei P09211.
    GeneWikii GSTP1.
    GenomeRNAii 2950.
    NextBioi 11692.
    PMAP-CutDB P09211.
    PROi P09211.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09211.
    Bgeei P09211.
    CleanExi HS_GSTP1.
    Genevestigatori P09211.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR003082. GST_pi.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01268. GSTRNSFRASEP.
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of a human class pi glutathione S-transferase messenger RNA."
      Kano T., Sakai M., Muramatsu M.
      Cancer Res. 47:5626-5630(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The structure of the human glutathione S-transferase pi gene."
      Cowell I.G., Dixon K.H., Pemble S.E., Ketterer B., Taylor J.B.
      Biochem. J. 255:79-83(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Structure of the human genomic glutathione S-transferase-pi gene."
      Morrow C.S., Cowan K.H., Goldsmith M.E.
      Gene 75:3-11(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Expression of anionic glutathione-S-transferase and P-glycoprotein genes in human tissues and tumors."
      Moscow J.A., Fairchild C.R., Madden M.J., Ransom D.T., Wieand H.S., O'Brien E.E., Poplack D.G., Cossman J., Myers C.E., Cowan K.H.
      Cancer Res. 49:1422-1428(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Human fatty acid ethyl ester synthase III gene: genomic organization, nucleotide sequence, genetic and chromosomal sublocalization."
      Bora P.S., Smith C., Lange L.G., Bora N.S., Jones C., Gerhard D.S.
      Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins."
      Ali-Osman F., Akande O., Antoun G., Mao J.X., Buolamwini J.
      J. Biol. Chem. 272:10004-10012(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-105 AND VAL-114.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. NIEHS SNPs program
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-105 AND VAL-114.
    10. "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], VARIANT VAL-105.
      Tissue: Urinary bladder.
    11. "Structural evidence for three different types of glutathione transferase in human tissues."
      Alin P., Mannervik B., Joernvall H.
      FEBS Lett. 182:319-322(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-24.
    12. "Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties."
      Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H.
      Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-24.
    13. "Purification and characterization of unique glutathione S-transferases from human muscle."
      Singh S.V., Ahmad H., Kurosky A., Awasthi Y.C.
      Arch. Biochem. Biophys. 264:13-22(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-14.
    14. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12.
      Tissue: Platelet.
    15. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 20-71; 76-101; 104-141; 122-141 AND 192-209, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    16. "A two-dimensional gel database of human colon carcinoma proteins."
      Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
      Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Colon carcinoma.
    17. "Primary and secondary structural analyses of glutathione S-transferase pi from human placenta."
      Ahmad H., Wilson D.E., Fritz R.R., Singh S.V., Medh R.D., Nagle G.T., Awasthi Y.C., Kurosky A.
      Arch. Biochem. Biophys. 278:398-408(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRIMARY AND SECONDARY STRUCTURAL ANALYZES.
    18. "Tyrosine-7 in human class Pi glutathione S-transferase is important for lowering the pKa of the thiol group of glutathione in the enzyme-glutathione complex."
      Kong K.H., Takasu K., Inoue H., Takahashi K.
      Biochem. Biophys. Res. Commun. 184:194-197(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-8.
    19. "Tyrosine-7 is an essential residue for the catalytic activity of human class PI glutathione S-transferase: chemical modification and site-directed mutagenesis studies."
      Kong K.H., Nishida M., Inoue H., Takahashi K.
      Biochem. Biophys. Res. Commun. 182:1122-1129(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-8.
    20. "Site-directed mutagenesis study on the roles of evolutionally conserved aspartic acid residues in human glutathione S-transferase P1-1."
      Kong K.-H., Inoue H., Takahashi K.
      Protein Eng. 6:93-99(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-99, CATALYTIC ACTIVITY.
    21. "Glutathione S-transferase pi localizes in mitochondria and protects against oxidative stress."
      Goto S., Kawakatsu M., Izumi S., Urata Y., Kageyama K., Ihara Y., Koji T., Kondo T.
      Free Radic. Biol. Med. 46:1392-1403(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    22. "Tyrosine phosphorylation of the human glutathione S-transferase P1 by epidermal growth factor receptor."
      Okamura T., Singh S., Buolamwini J., Haystead T., Friedman H., Bigner D., Ali-Osman F.
      J. Biol. Chem. 284:16979-16989(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-4 AND TYR-199.
    23. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase activity."
      Sun K.H., Chang K.H., Clawson S., Ghosh S., Mirzaei H., Regnier F., Shah K.
      J. Neurochem. 118:902-914(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDK5.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8-A resolution."
      Reinemer P., Dirr H.W., Ladenstein R., Huber R., Lo Bello M., Federici G., Parker M.W.
      J. Mol. Biol. 227:214-226(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) COMPLEX WITH S-HEXYLGLUTATHIONE.
    28. "The three-dimensional structure of the human Pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate."
      Oakley A.J., Rossjohn J., Lo Bello M., Caccuri A.M., Federici G., Parker M.W.
      Biochemistry 36:576-585(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR ETHACRYNIC ACID AND GLUTATHIONE.
    29. "Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase."
      Ji X., Tordova M., O'Donnell R., Parsons J.F., Hayden J.B., Gilliland G.L., Zimniak P.
      Biochemistry 36:9690-9702(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND INHIBITOR.
    30. "The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution."
      Oakley A.J., Lo Bello M., Battistoni A., Ricci G., Rossjohn J., Villar H.O., Parker M.W.
      J. Mol. Biol. 274:84-100(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE.
    31. "Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor."
      Prade L., Huber R., Manoharan T.H., Fahl W.E., Reuter W.
      Structure 5:1287-1295(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    32. "Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1."
      Ji X., Blaszczyk J., Xiao B., O'Donnell R., Hu X., Herzog C., Singh S.V., Zimniak P.
      Biochemistry 38:10231-10238(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    33. "Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure."
      Nicotra M., Paci M., Sette M., Oakley A.J., Parker M.W., Lo Bello M., Caccuri A.M., Federici G., Ricci G.
      Biochemistry 37:3020-3027(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    34. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    35. "Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases."
      Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F., Federici G., Caccuri A.M.
      Cancer Res. 69:8025-8034(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 2-210.

    Entry informationi

    Entry nameiGSTP1_HUMAN
    AccessioniPrimary (citable) accession number: P09211
    Secondary accession number(s): O00460, Q15690, Q5TZY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 177 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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

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