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P28161

- GSTM2_HUMAN

UniProt

P28161 - GSTM2_HUMAN

Protein

Glutathione S-transferase Mu 2

Gene

GSTM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (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.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei116 – 1161SubstrateBy similarity
    Sitei210 – 2101Important for substrate specificity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular detoxification of nitrogen compound Source: BHF-UCL
    2. cellular response to caffeine Source: BHF-UCL
    3. glutathione derivative biosynthetic process Source: Reactome
    4. glutathione metabolic process Source: UniProtKB
    5. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    6. nitrobenzene metabolic process Source: BHF-UCL
    7. positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    8. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
    9. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    10. regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: BHF-UCL
    11. relaxation of cardiac muscle Source: BHF-UCL
    12. small molecule metabolic process Source: Reactome
    13. xenobiotic catabolic process Source: UniProtKB
    14. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_6926. Glutathione conjugation.
    SABIO-RKP28161.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase Mu 2 (EC:2.5.1.18)
    Alternative name(s):
    GST class-mu 2
    GSTM2-2
    Gene namesi
    Name:GSTM2
    Synonyms:GST4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4634. GSTM2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. sarcoplasmic reticulum Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi210 – 2101T → C, F, H, I, K, L, R, Y or W: Reduced enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA29023.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 218217Glutathione S-transferase Mu 2PRO_0000185818Add
    BLAST

    Proteomic databases

    MaxQBiP28161.
    PaxDbiP28161.
    PRIDEiP28161.

    2D gel databases

    OGPiP28161.
    REPRODUCTION-2DPAGEP28161.

    PTM databases

    PhosphoSiteiP28161.

    Expressioni

    Tissue specificityi

    Muscle.

    Gene expression databases

    ArrayExpressiP28161.
    BgeeiP28161.
    CleanExiHS_GSTM2.
    GenevestigatoriP28161.

    Organism-specific databases

    HPAiCAB040547.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi109201. 3 interactions.
    DIPiDIP-129N.
    STRINGi9606.ENSP00000241337.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Helixi12 – 143
    Helixi15 – 239
    Beta strandi28 – 336
    Turni38 – 414
    Helixi44 – 474
    Turni48 – 514
    Beta strandi60 – 656
    Beta strandi68 – 725
    Helixi73 – 8311
    Helixi91 – 11626
    Helixi120 – 14223
    Beta strandi150 – 1523
    Helixi155 – 17016
    Turni172 – 1776
    Helixi179 – 19012
    Helixi192 – 1998
    Beta strandi200 – 2023
    Beta strandi205 – 2073
    Turni208 – 2125
    Beta strandi214 – 2163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HNAX-ray1.85A2-218[»]
    1HNBX-ray3.50A/B2-218[»]
    1HNCX-ray3.00A/B/C/D2-218[»]
    1XW5X-ray1.80A/B2-218[»]
    1YKCX-ray2.10A/B2-218[»]
    2AB6X-ray2.50A/B/C/D2-218[»]
    2C4JX-ray1.35A/B/C/D2-218[»]
    2GTUX-ray2.55A/B2-218[»]
    3GTUX-ray2.80A/C2-218[»]
    3GURX-ray2.50A/B/C/D2-218[»]
    ProteinModelPortaliP28161.
    SMRiP28161. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28161.

    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 binding
    Regioni46 – 505Glutathione binding
    Regioni59 – 602Glutathione binding
    Regioni72 – 732Glutathione binding

    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.
    OMAiWASGMAF.
    PhylomeDBiP28161.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P28161-1) [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

    MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK    50
    FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL 100
    ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG 150
    DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS 200
    SRFLPRPVFT KMAVWGNK 218
    Length:218
    Mass (Da):25,745
    Last modified:January 23, 2007 - v2
    Checksum:i15203709D4A63789
    GO
    Isoform 2 (identifier: P28161-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         190-218: GLEKISAYMKSSRFLPRPVFTKMAVWGNK → HS

    Note: No experimental confirmation available.

    Show »
    Length:191
    Mass (Da):22,644
    Checksum:i9267243C014F878F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21P → S in AAV38750. 1 PublicationCurated
    Sequence conflicti9 – 91N → D in AAV38750. 1 PublicationCurated
    Sequence conflicti51 – 511F → L in BAG61446. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti173 – 1731S → N.
    Corresponds to variant rs2229050 [ dbSNP | Ensembl ].
    VAR_049486

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei190 – 21829GLEKI…VWGNK → HS in isoform 2. CuratedVSP_045614Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63509 mRNA. Translation: AAA60963.1.
    AK299482 mRNA. Translation: BAG61446.1.
    BT019947 mRNA. Translation: AAV38750.1.
    AC000031 Genomic DNA. No translation available.
    AC000032 Genomic DNA. No translation available.
    BC105038 mRNA. Translation: AAI05039.1.
    BC105066 mRNA. Translation: AAI05067.1.
    CCDSiCCDS44192.1. [P28161-2]
    CCDS808.1. [P28161-1]
    PIRiA39375.
    RefSeqiNP_000839.1. NM_000848.3. [P28161-1]
    NP_001135840.1. NM_001142368.1. [P28161-2]
    UniGeneiHs.279837.

    Genome annotation databases

    EnsembliENST00000241337; ENSP00000241337; ENSG00000213366. [P28161-1]
    ENST00000442650; ENSP00000416883; ENSG00000213366. [P28161-2]
    ENST00000460717; ENSP00000435910; ENSG00000213366. [P28161-2]
    GeneIDi2946.
    KEGGihsa:2946.
    UCSCiuc001dyi.3. human. [P28161-1]
    uc010ovt.2. human.

    Polymorphism databases

    DMDMi232204.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63509 mRNA. Translation: AAA60963.1 .
    AK299482 mRNA. Translation: BAG61446.1 .
    BT019947 mRNA. Translation: AAV38750.1 .
    AC000031 Genomic DNA. No translation available.
    AC000032 Genomic DNA. No translation available.
    BC105038 mRNA. Translation: AAI05039.1 .
    BC105066 mRNA. Translation: AAI05067.1 .
    CCDSi CCDS44192.1. [P28161-2 ]
    CCDS808.1. [P28161-1 ]
    PIRi A39375.
    RefSeqi NP_000839.1. NM_000848.3. [P28161-1 ]
    NP_001135840.1. NM_001142368.1. [P28161-2 ]
    UniGenei Hs.279837.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HNA X-ray 1.85 A 2-218 [» ]
    1HNB X-ray 3.50 A/B 2-218 [» ]
    1HNC X-ray 3.00 A/B/C/D 2-218 [» ]
    1XW5 X-ray 1.80 A/B 2-218 [» ]
    1YKC X-ray 2.10 A/B 2-218 [» ]
    2AB6 X-ray 2.50 A/B/C/D 2-218 [» ]
    2C4J X-ray 1.35 A/B/C/D 2-218 [» ]
    2GTU X-ray 2.55 A/B 2-218 [» ]
    3GTU X-ray 2.80 A/C 2-218 [» ]
    3GUR X-ray 2.50 A/B/C/D 2-218 [» ]
    ProteinModelPortali P28161.
    SMRi P28161. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109201. 3 interactions.
    DIPi DIP-129N.
    STRINGi 9606.ENSP00000241337.

    Chemistry

    BindingDBi P28161.
    ChEMBLi CHEMBL4589.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei P28161.

    Polymorphism databases

    DMDMi 232204.

    2D gel databases

    OGPi P28161.
    REPRODUCTION-2DPAGE P28161.

    Proteomic databases

    MaxQBi P28161.
    PaxDbi P28161.
    PRIDEi P28161.

    Protocols and materials databases

    DNASUi 2946.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000241337 ; ENSP00000241337 ; ENSG00000213366 . [P28161-1 ]
    ENST00000442650 ; ENSP00000416883 ; ENSG00000213366 . [P28161-2 ]
    ENST00000460717 ; ENSP00000435910 ; ENSG00000213366 . [P28161-2 ]
    GeneIDi 2946.
    KEGGi hsa:2946.
    UCSCi uc001dyi.3. human. [P28161-1 ]
    uc010ovt.2. human.

    Organism-specific databases

    CTDi 2946.
    GeneCardsi GC01P110210.
    HGNCi HGNC:4634. GSTM2.
    HPAi CAB040547.
    MIMi 138380. gene.
    neXtProti NX_P28161.
    PharmGKBi PA29023.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300089.
    HOGENOMi HOG000115735.
    HOVERGENi HBG106842.
    KOi K00799.
    OMAi WASGMAF.
    PhylomeDBi P28161.
    TreeFami TF353040.

    Enzyme and pathway databases

    Reactomei REACT_6926. Glutathione conjugation.
    SABIO-RK P28161.

    Miscellaneous databases

    ChiTaRSi GSTM2. human.
    EvolutionaryTracei P28161.
    GeneWikii GSTM2.
    GenomeRNAii 2946.
    NextBioi 11674.
    PROi P28161.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28161.
    Bgeei P28161.
    CleanExi HS_GSTM2.
    Genevestigatori P28161.

    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. "Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus."
      Vorachek W.R., Pearson W.R., Rule G.S.
      Proc. Natl. Acad. Sci. U.S.A. 88:4443-4447(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Muscle.
    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].
      Tissue: Brain.
    3. "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] (ISOFORM 1).
    4. "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].
    5. "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: Brain.
    6. "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: PROTEIN SEQUENCE OF N-TERMINUS.
      Tissue: Testis.
    7. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 53-69 AND 153-182, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity."
      Raghunathan S., Chandross R.J., Kretsinger R.H., Allison T.J., Penington C.J., Rule G.S.
      J. Mol. Biol. 238:815-832(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.
    10. "Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution."
      Norrgard M.A., Ivarsson Y., Tars K., Mannervik B.
      Proc. Natl. Acad. Sci. U.S.A. 103:4876-4881(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, MUTAGENESIS OF THR-210, CATALYTIC ACTIVITY.
    11. "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 (2.5 ANGSTROMS) IN COMPLEX WITH NBDHEX.

    Entry informationi

    Entry nameiGSTM2_HUMAN
    AccessioniPrimary (citable) accession number: P28161
    Secondary accession number(s): B4DRY4
    , E9PEM9, Q2M318, Q5TZY5, Q8WWE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 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 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