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Q03013

- GSTM4_HUMAN

UniProt

Q03013 - GSTM4_HUMAN

Protein

Glutathione S-transferase Mu 4

Gene

GSTM4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 151 (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. Active on 1-chloro-2,4-dinitrobenzene.

    Catalytic activityi

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

    Sites

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

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. glutathione binding Source: BHF-UCL
    3. glutathione transferase activity Source: BHF-UCL
    4. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. glutathione derivative biosynthetic process Source: Reactome
    2. glutathione metabolic process Source: BHF-UCL
    3. small molecule metabolic process Source: Reactome
    4. xenobiotic catabolic process Source: BHF-UCL
    5. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_6926. Glutathione conjugation.
    SABIO-RKQ03013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase Mu 4 (EC:2.5.1.18)
    Alternative name(s):
    GST class-mu 4
    GST-Mu2
    GSTM4-4
    Gene namesi
    Name:GSTM4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4636. GSTM4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29026.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 218217Glutathione S-transferase Mu 4PRO_0000185824Add
    BLAST

    Proteomic databases

    MaxQBiQ03013.
    PaxDbiQ03013.
    PRIDEiQ03013.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00008770.

    PTM databases

    PhosphoSiteiQ03013.

    Expressioni

    Tissue specificityi

    Expressed in a wide variety of tissues.

    Gene expression databases

    ArrayExpressiQ03013.
    BgeeiQ03013.
    CleanExiHS_GSTM4.
    GenevestigatoriQ03013.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi109203. 12 interactions.
    IntActiQ03013. 9 interactions.
    MINTiMINT-1368381.
    STRINGi9606.ENSP00000358851.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Helixi14 – 2310
    Beta strandi28 – 336
    Turni38 – 414
    Helixi44 – 507
    Helixi51 – 533
    Beta strandi60 – 645
    Beta strandi69 – 724
    Helixi73 – 8311
    Helixi91 – 11424
    Helixi120 – 14223
    Beta strandi150 – 1523
    Helixi155 – 17016
    Helixi179 – 19012
    Helixi192 – 1987
    Turni214 – 2163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GTUX-ray3.30A/B/C/D/E/F/G/H2-218[»]
    ProteinModelPortaliQ03013.
    SMRiQ03013. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03013.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8887GST N-terminalAdd
    BLAST
    Domaini90 – 208119GST 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.
    InParanoidiQ03013.
    KOiK00799.
    OMAiLFACNIL.
    OrthoDBiEOG7KH9M3.
    PhylomeDBiQ03013.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q03013-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSMTLGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK    50
    FKLGLDFPNL PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL 100
    ENQAMDVSNQ LARVCYSPDF EKLKPEYLEE LPTMMQHFSQ FLGKRPWFVG 150
    DKITFVDFLA YDVLDLHRIF EPNCLDAFPN LKDFISRFEG LEKISAYMKS 200
    SRFLPKPLYT RVAVWGNK 218
    Length:218
    Mass (Da):25,561
    Last modified:January 23, 2007 - v3
    Checksum:i35E96FA54D566B1E
    GO
    Isoform 2 (identifier: Q03013-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         190-195: GLEKIS → VSCGIM
         196-218: Missing.

    Show »
    Length:195
    Mass (Da):22,829
    Checksum:i32F3BEF15BB378D3
    GO
    Isoform 3 (identifier: Q03013-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         60-120: Missing.

    Show »
    Length:157
    Mass (Da):18,627
    Checksum:i095AFD32871D3B4A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 43SMT → PMI in CAA48637. (PubMed:8471052)Curated
    Sequence conflicti17 – 171I → M in AAA57346. (PubMed:8349586)Curated
    Sequence conflicti37 – 371D → G in CAA48637. (PubMed:8471052)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21S → P.
    Corresponds to variant rs3211190 [ dbSNP | Ensembl ].
    VAR_033979
    Natural varianti160 – 1601A → V.
    Corresponds to variant rs17838158 [ dbSNP | Ensembl ].
    VAR_033980
    Natural varianti208 – 2081L → V.
    Corresponds to variant rs2229052 [ dbSNP | Ensembl ].
    VAR_049487
    Natural varianti209 – 2091Y → F.
    Corresponds to variant rs2229053 [ dbSNP | Ensembl ].
    VAR_049488
    Natural varianti211 – 2111R → K.
    Corresponds to variant rs2229054 [ dbSNP | Ensembl ].
    VAR_049489
    Natural varianti212 – 2121V → M.1 Publication
    Corresponds to variant rs1051113 [ dbSNP | Ensembl ].
    VAR_049490

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei60 – 12061Missing in isoform 3. 1 PublicationVSP_047688Add
    BLAST
    Alternative sequencei190 – 1956GLEKIS → VSCGIM in isoform 2. 1 PublicationVSP_011773
    Alternative sequencei196 – 21823Missing in isoform 2. 1 PublicationVSP_011774Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96234 mRNA. Translation: AAA57347.1.
    M96233 Genomic DNA. Translation: AAA57346.1.
    X68677 Genomic DNA. Translation: CAA48637.1.
    M99422 mRNA. Translation: AAA58623.1.
    DQ062813 mRNA. Translation: AAY98515.1.
    CR541869 mRNA. Translation: CAG46667.1.
    AK291880 mRNA. Translation: BAF84569.1.
    AC000031 Genomic DNA. No translation available.
    CH471122 Genomic DNA. Translation: EAW56405.1.
    BC015513 mRNA. Translation: AAH15513.1.
    BC108729 mRNA. Translation: AAI08730.1.
    X56837 Genomic DNA. Translation: CAA40167.1.
    CCDSiCCDS806.1. [Q03013-2]
    CCDS807.1. [Q03013-1]
    PIRiA47486.
    S32425.
    RefSeqiNP_000841.1. NM_000850.4. [Q03013-1]
    NP_671489.1. NM_147148.2. [Q03013-2]
    UniGeneiHs.348387.

    Genome annotation databases

    EnsembliENST00000326729; ENSP00000316471; ENSG00000168765. [Q03013-2]
    ENST00000336075; ENSP00000336744; ENSG00000168765. [Q03013-3]
    ENST00000369836; ENSP00000358851; ENSG00000168765. [Q03013-1]
    GeneIDi2948.
    KEGGihsa:2948.
    UCSCiuc001dyf.3. human. [Q03013-1]
    uc001dyh.2. human. [Q03013-2]

    Polymorphism databases

    DMDMi1170096.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96234 mRNA. Translation: AAA57347.1 .
    M96233 Genomic DNA. Translation: AAA57346.1 .
    X68677 Genomic DNA. Translation: CAA48637.1 .
    M99422 mRNA. Translation: AAA58623.1 .
    DQ062813 mRNA. Translation: AAY98515.1 .
    CR541869 mRNA. Translation: CAG46667.1 .
    AK291880 mRNA. Translation: BAF84569.1 .
    AC000031 Genomic DNA. No translation available.
    CH471122 Genomic DNA. Translation: EAW56405.1 .
    BC015513 mRNA. Translation: AAH15513.1 .
    BC108729 mRNA. Translation: AAI08730.1 .
    X56837 Genomic DNA. Translation: CAA40167.1 .
    CCDSi CCDS806.1. [Q03013-2 ]
    CCDS807.1. [Q03013-1 ]
    PIRi A47486.
    S32425.
    RefSeqi NP_000841.1. NM_000850.4. [Q03013-1 ]
    NP_671489.1. NM_147148.2. [Q03013-2 ]
    UniGenei Hs.348387.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GTU X-ray 3.30 A/B/C/D/E/F/G/H 2-218 [» ]
    ProteinModelPortali Q03013.
    SMRi Q03013. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109203. 12 interactions.
    IntActi Q03013. 9 interactions.
    MINTi MINT-1368381.
    STRINGi 9606.ENSP00000358851.

    Chemistry

    ChEMBLi CHEMBL2100.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei Q03013.

    Polymorphism databases

    DMDMi 1170096.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00008770.

    Proteomic databases

    MaxQBi Q03013.
    PaxDbi Q03013.
    PRIDEi Q03013.

    Protocols and materials databases

    DNASUi 2948.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326729 ; ENSP00000316471 ; ENSG00000168765 . [Q03013-2 ]
    ENST00000336075 ; ENSP00000336744 ; ENSG00000168765 . [Q03013-3 ]
    ENST00000369836 ; ENSP00000358851 ; ENSG00000168765 . [Q03013-1 ]
    GeneIDi 2948.
    KEGGi hsa:2948.
    UCSCi uc001dyf.3. human. [Q03013-1 ]
    uc001dyh.2. human. [Q03013-2 ]

    Organism-specific databases

    CTDi 2948.
    GeneCardsi GC01P110198.
    HGNCi HGNC:4636. GSTM4.
    MIMi 138333. gene.
    neXtProti NX_Q03013.
    PharmGKBi PA29026.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300089.
    HOGENOMi HOG000115735.
    HOVERGENi HBG106842.
    InParanoidi Q03013.
    KOi K00799.
    OMAi LFACNIL.
    OrthoDBi EOG7KH9M3.
    PhylomeDBi Q03013.
    TreeFami TF353040.

    Enzyme and pathway databases

    Reactomei REACT_6926. Glutathione conjugation.
    SABIO-RK Q03013.

    Miscellaneous databases

    EvolutionaryTracei Q03013.
    GeneWikii GSTM4.
    GenomeRNAii 2948.
    NextBioi 11682.
    PROi Q03013.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03013.
    Bgeei Q03013.
    CleanExi HS_GSTM4.
    Genevestigatori Q03013.

    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. "Isolation and analysis of the gene and cDNA for a human Mu class glutathione S-transferase, GSTM4."
      Comstock K.E., Johnson K.J., Rifenbery D., Henner W.D.
      J. Biol. Chem. 268:16958-16965(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    2. "Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4."
      Zhong S., Spurr N.K., Hayes J.D., Wolf C.R.
      Biochem. J. 291:41-50(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-212.
    3. "Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript."
      Ross V.L., Board P.G.
      Biochem. J. 294:373-380(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS.
      Tissue: Testis.
    4. "Screening for inter-individual splicing differences in human GSTM4 and the discovery of a single nucleotide substitution related to the tandem skipping of two exons."
      Denson J., Xi Z., Wu Y., Yang W., Neale G., Zhang J.
      Gene 379:148-155(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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] (ISOFORM 1).
      Tissue: Skeletal muscle.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 1).
      Tissue: Eye and Lung.
    10. "Structure of human glutathione S-transferase class Mu genes."
      Taylor J.B., Oliver J., Sherrington R., Pemble S.E.
      Biochem. J. 274:587-593(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-160.
      Tissue: Lymphocyte.
    11. "A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes."
      Comstock K.E., Widersten M., Hao X.Y., Henner W.D., Mannervik B.
      Arch. Biochem. Biophys. 311:487-495(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    12. "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: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).

    Entry informationi

    Entry nameiGSTM4_HUMAN
    AccessioniPrimary (citable) accession number: Q03013
    Secondary accession number(s): A8K765
    , Q05465, Q32NC1, Q4JNT8, Q6FH87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 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, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3