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P16455

- MGMT_HUMAN

UniProt

P16455 - MGMT_HUMAN

Protein

Methylated-DNA--protein-cysteine methyltransferase

Gene

MGMT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.

    Catalytic activityi

    DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine.PROSITE-ProRule annotation

    Cofactori

    Binds 1 zinc ion.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi5 – 51Zinc
    Metal bindingi24 – 241Zinc
    Metal bindingi29 – 291Zinc
    Metal bindingi85 – 851Zinc
    Binding sitei95 – 951DNA; via amide nitrogen2 Publications
    Binding sitei114 – 1141DNA2 Publications
    Binding sitei115 – 1151DNA; via amide nitrogen2 Publications
    Binding sitei123 – 1231DNA2 Publications
    Binding sitei128 – 1281DNA2 Publications
    Active sitei145 – 1451Nucleophile; methyl group acceptor
    Binding sitei151 – 1511DNA; via amide nitrogen2 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: Ensembl
    2. DNA binding Source: ProtInc
    3. DNA-methyltransferase activity Source: ProtInc
    4. methylated-DNA-[protein]-cysteine S-methyltransferase activity Source: UniProtKB-EC
    5. methyltransferase activity Source: ProtInc

    GO - Biological processi

    1. cellular response to ionizing radiation Source: Ensembl
    2. cellular response to organic cyclic compound Source: Ensembl
    3. cellular response to oxidative stress Source: Ensembl
    4. DNA dealkylation involved in DNA repair Source: Ensembl
    5. DNA ligation Source: ProtInc
    6. DNA methylation Source: GOC
    7. DNA repair Source: Reactome
    8. mammary gland epithelial cell differentiation Source: Ensembl
    9. negative regulation of cell death Source: Ensembl
    10. positive regulation of DNA repair Source: Ensembl
    11. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    12. response to drug Source: Ensembl
    13. response to ethanol Source: Ensembl
    14. response to folic acid Source: Ensembl
    15. response to toxic substance Source: Ensembl

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.1.1.63. 2681.
    ReactomeiREACT_127. DNA Damage Reversal.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylated-DNA--protein-cysteine methyltransferase (EC:2.1.1.63)
    Alternative name(s):
    6-O-methylguanine-DNA methyltransferase
    Short name:
    MGMT
    O-6-methylguanine-DNA-alkyltransferase
    Gene namesi
    Name:MGMT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:7059. MGMT.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141Y → A: Decreases activity towards methylated DNA over 1000-fold. Slightly reduced reactivity with O6-benzylguanine. 1 Publication
    Mutagenesisi114 – 1141Y → E: Loss of DNA repair activity. Slightly reduced reactivity with O6-benzylguanine. 1 Publication
    Mutagenesisi128 – 1281R → A or D: Decreases activity towards methylated DNA over 1000-fold. No effect on reactivity with O6-benzylguanine. 2 Publications
    Mutagenesisi128 – 1281R → G: Loss of DNA repair activity. 2 Publications
    Mutagenesisi128 – 1281R → K or L: Slightly reduced DNA repair activity. 2 Publications
    Mutagenesisi138 – 1381P → K: Decreased reactivity with O6-benzylguanine. 1 Publication
    Mutagenesisi140 – 1401P → A: Decreased reactivity with O6-benzylguanine. 1 Publication
    Mutagenesisi145 – 1451C → A: Loss of DNA repair activity. 2 Publications
    Mutagenesisi156 – 1561G → A: Decreased reactivity with O6-benzylguanine. 1 Publication
    Mutagenesisi158 – 1581Y → A: Reduced DNA repair activity. Decreased reactivity with O6-benzylguanine. 1 Publication
    Mutagenesisi158 – 1581Y → F: Slightly reduced DNA repair activity. 1 Publication

    Organism-specific databases

    Orphaneti251579. Giant cell glioblastoma.
    251576. Gliosarcoma.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 207207Methylated-DNA--protein-cysteine methyltransferasePRO_0000139359Add
    BLAST

    Proteomic databases

    MaxQBiP16455.
    PaxDbiP16455.
    PeptideAtlasiP16455.
    PRIDEiP16455.

    PTM databases

    PhosphoSiteiP16455.

    Expressioni

    Gene expression databases

    ArrayExpressiP16455.
    BgeeiP16455.
    CleanExiHS_MGMT.
    GenevestigatoriP16455.

    Organism-specific databases

    HPAiCAB002786.

    Interactioni

    Protein-protein interaction databases

    IntActiP16455. 1 interaction.
    MINTiMINT-5002466.
    STRINGi9606.ENSP00000302111.

    Structurei

    Secondary structure

    1
    207
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125
    Beta strandi19 – 246
    Beta strandi27 – 337
    Beta strandi50 – 523
    Helixi57 – 7115
    Helixi73 – 786
    Helixi87 – 904
    Helixi94 – 10512
    Helixi114 – 1207
    Turni124 – 1263
    Helixi127 – 1348
    Beta strandi138 – 1403
    Helixi145 – 1473
    Helixi162 – 17110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EH6X-ray2.00A1-207[»]
    1EH7X-ray2.00A1-207[»]
    1EH8X-ray2.50A1-207[»]
    1QNTX-ray1.90A1-176[»]
    1T38X-ray3.20A1-176[»]
    1T39X-ray3.30A/B1-176[»]
    1YFHX-ray3.01A/B/C1-179[»]
    ProteinModelPortaliP16455.
    SMRiP16455. Positions 6-176.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16455.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MGMT family.Curated

    Phylogenomic databases

    eggNOGiCOG0350.
    HOGENOMiHOG000244137.
    HOVERGENiHBG001146.
    InParanoidiP16455.
    KOiK00567.
    OrthoDBiEOG7RRF9D.
    PhylomeDBiP16455.
    TreeFamiTF314064.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR001497. MethylDNA_cys_MeTrfase_AS.
    IPR014048. MethylDNA_cys_MeTrfase_DNA-bd.
    IPR008332. MethylG_MeTrfase_N.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF01035. DNA_binding_1. 1 hit.
    PF02870. Methyltransf_1N. 1 hit.
    [Graphical view]
    SUPFAMiSSF46767. SSF46767. 1 hit.
    SSF53155. SSF53155. 1 hit.
    TIGRFAMsiTIGR00589. ogt. 1 hit.
    PROSITEiPS00374. MGMT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P16455-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKDCEMKRT TLDSPLGKLE LSGCEQGLHE IKLLGKGTSA ADAVEVPAPA    50
    AVLGGPEPLM QCTAWLNAYF HQPEAIEEFP VPALHHPVFQ QESFTRQVLW 100
    KLLKVVKFGE VISYQQLAAL AGNPKAARAV GGAMRGNPVP ILIPCHRVVC 150
    SSGAVGNYSG GLAVKEWLLA HEGHRLGKPG LGGSSGLAGA WLKGAGATSG 200
    SPPAGRN 207
    Length:207
    Mass (Da):21,646
    Last modified:August 1, 1990 - v1
    Checksum:i76BBF19DFC4512D6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1271A → T in AAA52317. (PubMed:2188979)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301E → K.
    Corresponds to variant rs2020893 [ dbSNP | Ensembl ].
    VAR_014750
    Natural varianti53 – 531L → F.
    Corresponds to variant rs12917 [ dbSNP | Ensembl ].
    VAR_056129
    Natural varianti58 – 581P → S.
    Corresponds to variant rs2308322 [ dbSNP | Ensembl ].
    VAR_029112
    Natural varianti65 – 651W → C.
    Corresponds to variant rs2282164 [ dbSNP | Ensembl ].
    VAR_020354
    Natural varianti84 – 841L → F.
    Corresponds to variant rs12917 [ dbSNP | Ensembl ].
    VAR_014751
    Natural varianti112 – 1121I → V.
    Corresponds to variant rs2308321 [ dbSNP | Ensembl ].
    VAR_056130
    Natural varianti143 – 1431I → V.
    Corresponds to variant rs2308321 [ dbSNP | Ensembl ].
    VAR_014752
    Natural varianti160 – 1601G → R.
    Corresponds to variant rs2308318 [ dbSNP | Ensembl ].
    VAR_014753
    Natural varianti166 – 1661E → D.
    Corresponds to variant rs2308320 [ dbSNP | Ensembl ].
    VAR_014754
    Natural varianti178 – 1781K → R.
    Corresponds to variant rs2308327 [ dbSNP | Ensembl ].
    VAR_014755

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54228 mRNA. Translation: CAA38137.1.
    M29971 mRNA. Translation: AAA59596.1.
    M31767 mRNA. Translation: AAA52317.1.
    M60761 mRNA. Translation: AAA59594.1.
    BT006714 mRNA. Translation: AAP35360.1.
    AL157832, AL355531 Genomic DNA. Translation: CAH70060.1.
    AL355531, AL157832 Genomic DNA. Translation: CAH72190.1.
    CH471066 Genomic DNA. Translation: EAW49166.1.
    BC000824 mRNA. Translation: AAH00824.1.
    PIRiA34889. XUHUMC.
    RefSeqiXP_005252739.1. XM_005252682.1.
    UniGeneiHs.501522.

    Genome annotation databases

    EnsembliENST00000306010; ENSP00000302111; ENSG00000170430.
    GeneIDi4255.
    KEGGihsa:4255.

    Polymorphism databases

    DMDMi127069.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54228 mRNA. Translation: CAA38137.1 .
    M29971 mRNA. Translation: AAA59596.1 .
    M31767 mRNA. Translation: AAA52317.1 .
    M60761 mRNA. Translation: AAA59594.1 .
    BT006714 mRNA. Translation: AAP35360.1 .
    AL157832 , AL355531 Genomic DNA. Translation: CAH70060.1 .
    AL355531 , AL157832 Genomic DNA. Translation: CAH72190.1 .
    CH471066 Genomic DNA. Translation: EAW49166.1 .
    BC000824 mRNA. Translation: AAH00824.1 .
    PIRi A34889. XUHUMC.
    RefSeqi XP_005252739.1. XM_005252682.1.
    UniGenei Hs.501522.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EH6 X-ray 2.00 A 1-207 [» ]
    1EH7 X-ray 2.00 A 1-207 [» ]
    1EH8 X-ray 2.50 A 1-207 [» ]
    1QNT X-ray 1.90 A 1-176 [» ]
    1T38 X-ray 3.20 A 1-176 [» ]
    1T39 X-ray 3.30 A/B 1-176 [» ]
    1YFH X-ray 3.01 A/B/C 1-179 [» ]
    ProteinModelPortali P16455.
    SMRi P16455. Positions 6-176.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P16455. 1 interaction.
    MINTi MINT-5002466.
    STRINGi 9606.ENSP00000302111.

    Chemistry

    BindingDBi P16455.
    ChEMBLi CHEMBL2864.
    DrugBanki DB00151. L-Cysteine.

    PTM databases

    PhosphoSitei P16455.

    Polymorphism databases

    DMDMi 127069.

    Proteomic databases

    MaxQBi P16455.
    PaxDbi P16455.
    PeptideAtlasi P16455.
    PRIDEi P16455.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306010 ; ENSP00000302111 ; ENSG00000170430 .
    GeneIDi 4255.
    KEGGi hsa:4255.

    Organism-specific databases

    CTDi 4255.
    GeneCardsi GC10P131195.
    H-InvDB HIX0009309.
    HGNCi HGNC:7059. MGMT.
    HPAi CAB002786.
    MIMi 156569. gene.
    neXtProti NX_P16455.
    Orphaneti 251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0350.
    HOGENOMi HOG000244137.
    HOVERGENi HBG001146.
    InParanoidi P16455.
    KOi K00567.
    OrthoDBi EOG7RRF9D.
    PhylomeDBi P16455.
    TreeFami TF314064.

    Enzyme and pathway databases

    BRENDAi 2.1.1.63. 2681.
    Reactomei REACT_127. DNA Damage Reversal.

    Miscellaneous databases

    EvolutionaryTracei P16455.
    GeneWikii O-6-methylguanine-DNA_methyltransferase.
    GenomeRNAii 4255.
    PROi P16455.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16455.
    Bgeei P16455.
    CleanExi HS_MGMT.
    Genevestigatori P16455.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR001497. MethylDNA_cys_MeTrfase_AS.
    IPR014048. MethylDNA_cys_MeTrfase_DNA-bd.
    IPR008332. MethylG_MeTrfase_N.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF01035. DNA_binding_1. 1 hit.
    PF02870. Methyltransf_1N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46767. SSF46767. 1 hit.
    SSF53155. SSF53155. 1 hit.
    TIGRFAMsi TIGR00589. ogt. 1 hit.
    PROSITEi PS00374. MGMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and structural characterization of a cDNA clone encoding the human DNA repair protein for O6-alkylguanine."
      Tano K., Shiota S., Collier J., Foote R.S., Mitra S.
      Proc. Natl. Acad. Sci. U.S.A. 87:686-690(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-8.
    2. "cDNA cloning and chromosomal assignment of the human O6-methylguanine-DNA methyltransferase. cDNA expression in Escherichia coli and gene expression in human cells."
      Rydberg B., Spurr N., Karran P.
      J. Biol. Chem. 265:9563-9569(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Purification, structure, and biochemical properties of human O6-methylguanine-DNA methyltransferase."
      Koike G., Maki H., Takeya H., Hayakawa H., Sekiguchi M.
      J. Biol. Chem. 265:14754-14762(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Expression and cloning of complementary DNA for a human enzyme that repairs O6-methylguanine in DNA."
      Hayakawa H., Koike G., Sekiguchi M.
      J. Mol. Biol. 213:739-747(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: Placenta.
    9. "Structural and immunological comparison of indigenous human O6-methylguanine-DNA methyltransferase with that encoded by a cloned cDNA."
      von Wronski M.A., Shiota S., Tano K., Mitra S., Bigner D.D., Brent T.P.
      J. Biol. Chem. 266:1064-1070(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, ALKYL GROUP ACCEPTOR.
    10. "Specificities of human, rat and E. coli O6-methylguanine-DNA methyltransferases towards the repair of O6-methyl and O6-ethylguanine in DNA."
      Liem L.-K., Lim A., Li B.F.L.
      Nucleic Acids Res. 22:1613-1619(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "Mutations in human O6-alkylguanine-DNA alkyltransferase imparting resistance to O6-benzylguanine."
      Crone T.M., Goodtzova K., Edara S., Pegg A.E.
      Cancer Res. 54:6221-6227(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-138; PRO-140 AND GLY-156.
    12. "Alteration of arginine-128 to alanine abolishes the ability of human O6-alkylguanine-DNA alkyltransferase to repair methylated DNA but has no effect on its reaction with O6-benzylguanine."
      Kanugula S., Goodtzova K., Edara S., Pegg A.E.
      Biochemistry 34:7113-7119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-114; ARG-128 AND CYS-145.
    13. "The role of tyrosine-158 in O6-alkylguanine-DNA alkyltransferase activity."
      Edara S., Goodtzova K., Pegg A.E.
      Carcinogenesis 16:1637-1642(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-158.
    14. "Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding."
      Daniels D.S., Mol C.D., Arvai A.S., Kanugula S., Pegg A.E., Tainer J.A.
      EMBO J. 19:1719-1730(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH DNA AND ZINC IONS, MUTAGENESIS OF ARG-128 AND CYS-145.
    15. "Crystal structure of the human O(6)-alkylguanine-DNA alkyltransferase."
      Wibley J.E., Pegg A.E., Moody P.C.
      Nucleic Acids Res. 28:393-401(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-176.
    16. "The structure of the human AGT protein bound to DNA and its implications for damage detection."
      Duguid E.M., Rice P.A., He C.
      J. Mol. Biol. 350:657-666(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-179 IN COMPLEX WITH DNA AND ZINC IONS.

    Entry informationi

    Entry nameiMGMT_HUMAN
    AccessioniPrimary (citable) accession number: P16455
    Secondary accession number(s): Q5VY78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 155 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

    Miscellaneous

    This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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