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UniProtKB/Swiss-Prot entry P24528

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MGMT_RAT
Primary accession number P24528
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 63)
Name and origin of the protein
Protein name Methylated-DNA--protein-cysteine methyltransferase
Synonyms EC 2.1.1.63
6-O-methylguanine-DNA methyltransferase
MGMT
O-6-methylguanine-DNA-alkyltransferase
Gene name
Name: Mgmt
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0006-291X(91)91830-6; PubMed=2049083 [NCBI, ExPASy, EBI, Israel, Japan]
Rahden-Staron I., Laval F.;
"cDNA cloning of the rat O6-methylguanine-DNA-methyltransferase.";
Biochem. Biophys. Res. Commun. 177:597-602(1991).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1093/carcin/12.4.727; PubMed=2013136 [NCBI, ExPASy, EBI, Israel, Japan]
Potter P.M., Rafferty J.A., Cawkwell L., Wilkinson M.C., Cooper D.P., O'Connor P.J., Margison G.P.;
"Isolation and cDNA cloning of a rat O6-alkylguanine-DNA-alkyltransferase gene, molecular analysis of expression in rat liver.";
Carcinogenesis 12:727-733(1991).
[3]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8467487 [NCBI, ExPASy, EBI, Israel, Japan]
Potter P.M., Harris L.C., Remack J.S., Edwards C.C., Brent T.P.;
"Ribozyme-mediated modulation of human O6-methylguanine-DNA methyltransferase expression.";
Cancer Res. 53:1731-1734(1993).
[4]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/19.20.5597; PubMed=1945835 [NCBI, ExPASy, EBI, Israel, Japan]
Sakumi K., Shiraishi A., Hayakawa H., Sekiguchi M.;
"Cloning and expresion of cDNA for rat O6-methylguanine-DNA methyltransferase.";
Nucleic Acids Res. 19:5597-5601(1991).
[5]
 CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1093/nar/22.9.1613; PubMed=8202360 [NCBI, ExPASy, EBI, Israel, Japan]
Liem L.-K., Lim A., Li B.F.L.;
"Specificities of human, rat and E. coli O6-methylguanine-DNA methyltransferases towards the repair of O6-methyl and O6-ethylguanine in DNA.";
Nucleic Acids Res. 22:1613-1619(1994).
Comments
  • FUNCTION: 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 ACTIVITY: DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine.
  • COFACTOR: Binds 1 zinc ion (By similarity).
  • SUBCELLULAR LOCATION: Nucleus (Probable).
  • SIMILARITY: Belongs to the MGMT family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
S61804; AAB20187.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M76704; AAA42052.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54862; CAA38648.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JN0071; XURTMC.
RefSeq NP_036993.1; -.
UniGene Rn.9836
3D structure databases
HSSP P16455; 1EH7. [HSSP ENTRY / PDB]
SMR P24528; 6-178.
ModBase P24528.
Organism-specific databases
RGD 3087; Mgmt.
Gene expression databases
ArrayExpress P24528; -.
GermOnline ENSRNOG00000016038; Rattus norvegicus.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003908; Molecular function: methylated-DNA-[protein]-cysteine S-methyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001497; MethylDNA_cys_MeTrfase_AS.
IPR014048; MethylDNA_cys_MeTrfase_DNA_bd.
IPR008332; MethylG_MeTrfase.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
PANTHER PTHR10815; MethylDNA_cys_mtrans_DNA_bd; 1.
Pfam PF01035; DNA_binding_1; 1.
PF02870; Methyltransf_1N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00589; ogt; 1.
PROSITE PS00374; MGMT; 1.
BLOCKS P24528.
ProtoNet P24528.
Genome annotation databases
Ensembl ENSRNOG00000016038; Rattus norvegicus. [Contig view]
GeneID 25332; -.
KEGG rno:25332; -.
NMPDR fig|10116.3.peg.3168; -.
Phylogenomic databases
HOVERGEN P24528; -.
Other
NextBio 606215; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; DNA damage; DNA repair; DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   209  208     Methylated-DNA--protein-cysteine methyltransferase. PRO_0000139361
ACT_SITE   149   149        Nucleophile; methyl group acceptor (By similarity). 
METAL   5     5        Zinc (By similarity). 
METAL   24    24        Zinc (By similarity). 
METAL   29    29        Zinc (By similarity). 
METAL   89    89        Zinc (By similarity). 
BINDING   99    99        DNA; via amide nitrogen (By similarity). 
BINDING   118   118        DNA (By similarity). 
BINDING   119   119        DNA; via amide nitrogen (By similarity). 
BINDING   127   127        DNA (By similarity). 
BINDING   132   132        DNA (By similarity). 
BINDING   155   155        DNA; via amide nitrogen (By similarity). 
MOD_RES   10    10        Phosphothreonine (By similarity). 
Sequence information
Length: 209 AA [This is the length of the unprocessed precursor] Molecular weight: 22244 Da [This is the MW of the unprocessed precursor] CRC64: 61F8F51C8937D4A7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAEICKMKYT VLDSPLGKIE LSGCERGLHG IRFLSGKTPN TDPTEAPACP EVLGGPEGVP 

        70         80         90        100        110        120 
EPLVQCTAWL EAYFHEPAAT EGLPLPALHH PVFQQDSFTR QVLWKLLKVV KFGEMVSYQQ 

       130        140        150        160        170        180 
LAALAGNPKA ARAVGGAMRS NPVPILIPCH RVIRSDGAIG NYSGGGQTVK EWLLAHEGIP 

       190        200 
TGQPASKGLG LIGSWLKPSF ESSSPKPSG
P24528 in FASTA format

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