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Q7RTV2

- GSTA5_HUMAN

UniProt

Q7RTV2 - GSTA5_HUMAN

Protein

Glutathione S-transferase A5

Gene

GSTA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91GlutathioneBy similarity
    Binding sitei45 – 451GlutathioneBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB

    GO - Biological processi

    1. glutathione metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_6926. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase A5 (EC:2.5.1.18)
    Alternative name(s):
    GST class-alpha member 5
    Glutathione S-transferase A5-5
    Gene namesi
    Name:GSTA5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:19662. GSTA5.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134962856.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 222221Glutathione S-transferase A5PRO_0000185787Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei4 – 41N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ7RTV2.
    PRIDEiQ7RTV2.

    PTM databases

    PhosphoSiteiQ7RTV2.

    Expressioni

    Tissue specificityi

    Expression not detected.

    Gene expression databases

    BgeeiQ7RTV2.
    CleanExiHS_GSTA5.
    GenevestigatoriQ7RTV2.

    Organism-specific databases

    HPAiHPA004342.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi9606.ENSP00000284562.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7RTV2.
    SMRiQ7RTV2. Positions 2-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8381GST N-terminalAdd
    BLAST
    Domaini85 – 208124GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 552Glutathione bindingBy similarity
    Regioni67 – 682Glutathione bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG266414.
    HOGENOMiHOG000115734.
    HOVERGENiHBG053749.
    InParanoidiQ7RTV2.
    KOiK00799.
    OMAiICQPEER.
    OrthoDBiEOG79CZ0K.
    PhylomeDBiQ7RTV2.
    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.
    IPR003080. GST_alpha.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01266. GSTRNSFRASEA.
    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.

    Q7RTV2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEKPKLHYS NARGSMESIR WLLAAAGVEL EEKFLESAED LDKLRNDGSL    50
    LFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDMKERA LIDMYTEGIV 100
    DLTEMILLLL ICQPEERDAK TALVKEKIKN RYFPAFEKVL KSHRQDYLVG 150
    NKLSWADIHL VELFYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP 200
    GSQRKPPMDE KSLEEARKIF RF 222
    Length:222
    Mass (Da):25,722
    Last modified:December 15, 2003 - v1
    Checksum:i6DFCECF202F2D898
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551V → I.
    Corresponds to variant rs2397118 [ dbSNP | Ensembl ].
    VAR_024483

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL590363 Genomic DNA. Translation: CAI13814.1.
    BK000212 Genomic DNA. Translation: DAA00071.1.
    CCDSiCCDS4946.1.
    RefSeqiNP_714543.1. NM_153699.1.
    UniGeneiHs.646984.

    Genome annotation databases

    EnsembliENST00000284562; ENSP00000284562; ENSG00000182793.
    ENST00000370989; ENSP00000360028; ENSG00000182793.
    GeneIDi221357.
    KEGGihsa:221357.
    UCSCiuc003pba.1. human.

    Polymorphism databases

    DMDMi50400409.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL590363 Genomic DNA. Translation: CAI13814.1 .
    BK000212 Genomic DNA. Translation: DAA00071.1 .
    CCDSi CCDS4946.1.
    RefSeqi NP_714543.1. NM_153699.1.
    UniGenei Hs.646984.

    3D structure databases

    ProteinModelPortali Q7RTV2.
    SMRi Q7RTV2. Positions 2-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000284562.

    Chemistry

    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei Q7RTV2.

    Polymorphism databases

    DMDMi 50400409.

    Proteomic databases

    PaxDbi Q7RTV2.
    PRIDEi Q7RTV2.

    Protocols and materials databases

    DNASUi 221357.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284562 ; ENSP00000284562 ; ENSG00000182793 .
    ENST00000370989 ; ENSP00000360028 ; ENSG00000182793 .
    GeneIDi 221357.
    KEGGi hsa:221357.
    UCSCi uc003pba.1. human.

    Organism-specific databases

    CTDi 221357.
    GeneCardsi GC06M052696.
    HGNCi HGNC:19662. GSTA5.
    HPAi HPA004342.
    MIMi 607605. gene.
    neXtProti NX_Q7RTV2.
    PharmGKBi PA134962856.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266414.
    HOGENOMi HOG000115734.
    HOVERGENi HBG053749.
    InParanoidi Q7RTV2.
    KOi K00799.
    OMAi ICQPEER.
    OrthoDBi EOG79CZ0K.
    PhylomeDBi Q7RTV2.
    TreeFami TF105321.

    Enzyme and pathway databases

    Reactomei REACT_6926. Glutathione conjugation.

    Miscellaneous databases

    GenomeRNAii 221357.
    NextBioi 91297.
    PROi Q7RTV2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q7RTV2.
    CleanExi HS_GSTA5.
    Genevestigatori Q7RTV2.

    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.
    IPR003080. GST_alpha.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01266. GSTRNSFRASEA.
    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. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter."
      Morel F., Rauch C., Coles B., Ferrec E.L., Guillouzo A.
      Pharmacogenetics 12:277-286(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    3. "The human hGSTA5 gene encodes an enzymatically active protein."
      Singh S.P., Zimniak L., Zimniak P.
      Biochim. Biophys. Acta 1800:16-22(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiGSTA5_HUMAN
    AccessioniPrimary (citable) accession number: Q7RTV2
    Secondary accession number(s): Q5SZC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3