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P16455

- MGMT_HUMAN

UniProt

P16455 - MGMT_HUMAN

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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

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

Zn2+Note: 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP16455.
CleanExiHS_MGMT.
ExpressionAtlasiP16455. baseline and differential.
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 – 125Combined sources
Beta strandi19 – 246Combined sources
Beta strandi27 – 337Combined sources
Beta strandi50 – 523Combined sources
Helixi57 – 7115Combined sources
Helixi73 – 786Combined sources
Helixi87 – 904Combined sources
Helixi94 – 10512Combined sources
Helixi114 – 1207Combined sources
Turni124 – 1263Combined sources
Helixi127 – 1348Combined sources
Beta strandi138 – 1403Combined sources
Helixi145 – 1473Combined sources
Helixi162 – 17110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MDKDCEMKRT TLDSPLGKLE LSGCEQGLHE IKLLGKGTSA ADAVEVPAPA
60 70 80 90 100
AVLGGPEPLM QCTAWLNAYF HQPEAIEEFP VPALHHPVFQ QESFTRQVLW
110 120 130 140 150
KLLKVVKFGE VISYQQLAAL AGNPKAARAV GGAMRGNPVP ILIPCHRVVC
160 170 180 190 200
SSGAVGNYSG GLAVKEWLLA HEGHRLGKPG LGGSSGLAGA WLKGAGATSG

SPPAGRN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

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

Gene expression databases

Bgeei P16455.
CleanExi HS_MGMT.
ExpressionAtlasi P16455. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 157 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