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P46439

- GSTM5_HUMAN

UniProt

P46439 - GSTM5_HUMAN

Protein

Glutathione S-transferase Mu 5

Gene

GSTM5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (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.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei116 – 1161SubstrateBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB

    GO - Biological processi

    1. glutathione derivative biosynthetic process Source: Reactome
    2. glutathione metabolic process Source: UniProtKB
    3. small molecule metabolic process Source: Reactome
    4. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_6926. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase Mu 5 (EC:2.5.1.18)
    Alternative name(s):
    GST class-mu 5
    GSTM5-5
    Gene namesi
    Name:GSTM5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4637. GSTM5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29027.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 218218Glutathione S-transferase Mu 5PRO_0000185825Add
    BLAST

    Proteomic databases

    PaxDbiP46439.
    PRIDEiP46439.

    PTM databases

    PhosphoSiteiP46439.

    Expressioni

    Gene expression databases

    ArrayExpressiP46439.
    BgeeiP46439.
    CleanExiHS_GSTM5.
    GenevestigatoriP46439.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi109204. 2 interactions.
    IntActiP46439. 1 interaction.
    STRINGi9606.ENSP00000256593.

    Structurei

    3D structure databases

    ProteinModelPortaliP46439.
    SMRiP46439. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8887GST N-terminalAdd
    BLAST
    Domaini90 – 207118GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 82Glutathione bindingBy similarity
    Regioni46 – 505Glutathione bindingBy similarity
    Regioni59 – 602Glutathione bindingBy similarity
    Regioni72 – 732Glutathione bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG300089.
    HOGENOMiHOG000115735.
    HOVERGENiHBG106842.
    KOiK00799.
    OrthoDBiEOG7KH9M3.
    PhylomeDBiP46439.
    TreeFamiTF353040.

    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.
    IPR003081. GST_mu.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01267. GSTRNSFRASEM.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P46439-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPMTLGYWDI RGLAHAIRLL LEYTDSSYVE KKYTLGDAPD YDRSQWLNEK    50
    FKLGLDFPNL PYLIDGAHKI TQSNAILRYI ARKHNLCGET EEEKIRVDIL 100
    ENQVMDNHME LVRLCYDPDF EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG 150
    DKITFVDFLA YDVLDMKRIF EPKCLDAFLN LKDFISRFEG LKKISAYMKS 200
    SQFLRGLLFG KSATWNSK 218
    Length:218
    Mass (Da):25,675
    Last modified:January 23, 2007 - v3
    Checksum:i62B03FCD960FB4AB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351L → M in AAA20040. (PubMed:8473333)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671A → T.2 Publications
    Corresponds to variant rs17854972 [ dbSNP | Ensembl ].
    VAR_065098
    Natural varianti179 – 1791L → P.
    Corresponds to variant rs2227963 [ dbSNP | Ensembl ].
    VAR_049491

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02321 mRNA. Translation: AAA20040.1.
    AK289673 mRNA. Translation: BAF82362.1.
    BC058881 mRNA. Translation: AAH58881.1.
    CCDSiCCDS811.1.
    PIRiA46048.
    RefSeqiNP_000842.2. NM_000851.3.
    XP_005270841.1. XM_005270784.2.
    UniGeneiHs.75652.

    Genome annotation databases

    EnsembliENST00000256593; ENSP00000256593; ENSG00000134201.
    GeneIDi2949.
    KEGGihsa:2949.
    UCSCiuc001dyn.3. human.

    Polymorphism databases

    DMDMi67476963.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02321 mRNA. Translation: AAA20040.1 .
    AK289673 mRNA. Translation: BAF82362.1 .
    BC058881 mRNA. Translation: AAH58881.1 .
    CCDSi CCDS811.1.
    PIRi A46048.
    RefSeqi NP_000842.2. NM_000851.3.
    XP_005270841.1. XM_005270784.2.
    UniGenei Hs.75652.

    3D structure databases

    ProteinModelPortali P46439.
    SMRi P46439. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109204. 2 interactions.
    IntActi P46439. 1 interaction.
    STRINGi 9606.ENSP00000256593.

    Chemistry

    ChEMBLi CHEMBL2819.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei P46439.

    Polymorphism databases

    DMDMi 67476963.

    Proteomic databases

    PaxDbi P46439.
    PRIDEi P46439.

    Protocols and materials databases

    DNASUi 2949.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256593 ; ENSP00000256593 ; ENSG00000134201 .
    GeneIDi 2949.
    KEGGi hsa:2949.
    UCSCi uc001dyn.3. human.

    Organism-specific databases

    CTDi 2949.
    GeneCardsi GC01P110256.
    HGNCi HGNC:4637. GSTM5.
    MIMi 138385. gene.
    neXtProti NX_P46439.
    PharmGKBi PA29027.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300089.
    HOGENOMi HOG000115735.
    HOVERGENi HBG106842.
    KOi K00799.
    OrthoDBi EOG7KH9M3.
    PhylomeDBi P46439.
    TreeFami TF353040.

    Enzyme and pathway databases

    Reactomei REACT_6926. Glutathione conjugation.

    Miscellaneous databases

    GenomeRNAii 2949.
    NextBioi 11688.
    PROi P46439.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46439.
    Bgeei P46439.
    CleanExi HS_GSTM5.
    Genevestigatori P46439.

    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.
    IPR003081. GST_mu.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01267. GSTRNSFRASEM.
    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. "A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5."
      Takahashi Y., Campbell E.A., Hirata Y., Takayama T., Listowsky I.
      J. Biol. Chem. 268:8893-8898(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-67.
      Tissue: Amygdala.
    3. "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 THR-67.
      Tissue: PNS.
    4. "An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases."
      Patskovsky Y.V., Patskovska L.N., Listowsky I.
      Biochemistry 38:16187-16194(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiGSTM5_HUMAN
    AccessioniPrimary (citable) accession number: P46439
    Secondary accession number(s): A8K0V8, Q6PD78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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