MGMT_HUMAN
ID MGMT_HUMAN Reviewed; 207 AA.
AC P16455; Q5VY78;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase;
DE EC=2.1.1.63;
DE AltName: Full=6-O-methylguanine-DNA methyltransferase;
DE Short=MGMT;
DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase;
GN Name=MGMT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-8.
RX PubMed=2405387; DOI=10.1073/pnas.87.2.686;
RA Tano K., Shiota S., Collier J., Foote R.S., Mitra S.;
RT "Isolation and structural characterization of a cDNA clone encoding the
RT human DNA repair protein for O6-alkylguanine.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:686-690(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2188979; DOI=10.1016/s0021-9258(19)38885-4;
RA Rydberg B., Spurr N., Karran P.;
RT "cDNA cloning and chromosomal assignment of the human O6-methylguanine-DNA
RT methyltransferase. cDNA expression in Escherichia coli and gene expression
RT in human cells.";
RL J. Biol. Chem. 265:9563-9569(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2394694; DOI=10.1016/s0021-9258(18)77177-9;
RA Koike G., Maki H., Takeya H., Hayakawa H., Sekiguchi M.;
RT "Purification, structure, and biochemical properties of human O6-
RT methylguanine-DNA methyltransferase.";
RL J. Biol. Chem. 265:14754-14762(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2359121; DOI=10.1016/s0022-2836(05)80260-8;
RA Hayakawa H., Koike G., Sekiguchi M.;
RT "Expression and cloning of complementary DNA for a human enzyme that
RT repairs O6-methylguanine in DNA.";
RL J. Mol. Biol. 213:739-747(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PARTIAL PROTEIN SEQUENCE, AND ALKYL GROUP ACCEPTOR.
RX PubMed=1985934; DOI=10.1016/s0021-9258(17)35283-3;
RA von Wronski M.A., Shiota S., Tano K., Mitra S., Bigner D.D., Brent T.P.;
RT "Structural and immunological comparison of indigenous human O6-
RT methylguanine-DNA methyltransferase with that encoded by a cloned cDNA.";
RL J. Biol. Chem. 266:1064-1070(1991).
RN [10]
RP CHARACTERIZATION.
RX PubMed=8202360; DOI=10.1093/nar/22.9.1613;
RA Liem L.-K., Lim A., Li B.F.L.;
RT "Specificities of human, rat and E. coli O6-methylguanine-DNA
RT methyltransferases towards the repair of O6-methyl and O6-ethylguanine in
RT DNA.";
RL Nucleic Acids Res. 22:1613-1619(1994).
RN [11]
RP MUTAGENESIS OF PRO-138; PRO-140 AND GLY-156.
RX PubMed=7954470;
RA Crone T.M., Goodtzova K., Edara S., Pegg A.E.;
RT "Mutations in human O6-alkylguanine-DNA alkyltransferase imparting
RT resistance to O6-benzylguanine.";
RL Cancer Res. 54:6221-6227(1994).
RN [12]
RP MUTAGENESIS OF TYR-114; ARG-128 AND CYS-145.
RX PubMed=7766621; DOI=10.1021/bi00021a024;
RA Kanugula S., Goodtzova K., Edara S., Pegg A.E.;
RT "Alteration of arginine-128 to alanine abolishes the ability of human O6-
RT alkylguanine-DNA alkyltransferase to repair methylated DNA but has no
RT effect on its reaction with O6-benzylguanine.";
RL Biochemistry 34:7113-7119(1995).
RN [13]
RP MUTAGENESIS OF TYR-158.
RX PubMed=7614699; DOI=10.1093/carcin/16.7.1637;
RA Edara S., Goodtzova K., Pegg A.E.;
RT "The role of tyrosine-158 in O6-alkylguanine-DNA alkyltransferase
RT activity.";
RL Carcinogenesis 16:1637-1642(1995).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH DNA AND ZINC IONS,
RP AND MUTAGENESIS OF ARG-128 AND CYS-145.
RX PubMed=10747039; DOI=10.1093/emboj/19.7.1719;
RA Daniels D.S., Mol C.D., Arvai A.S., Kanugula S., Pegg A.E., Tainer J.A.;
RT "Active and alkylated human AGT structures: a novel zinc site, inhibitor
RT and extrahelical base binding.";
RL EMBO J. 19:1719-1730(2000).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-176.
RX PubMed=10606635; DOI=10.1093/nar/28.2.393;
RA Wibley J.E., Pegg A.E., Moody P.C.;
RT "Crystal structure of the human O(6)-alkylguanine-DNA alkyltransferase.";
RL Nucleic Acids Res. 28:393-401(2000).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-179 IN COMPLEX WITH DNA AND ZINC
RP IONS.
RX PubMed=15964013; DOI=10.1016/j.jmb.2005.05.028;
RA Duguid E.M., Rice P.A., He C.;
RT "The structure of the human AGT protein bound to DNA and its implications
RT for damage detection.";
RL J. Mol. Biol. 350:657-666(2005).
CC -!- FUNCTION: Involved in the cellular defense against the biological
CC effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in
CC DNA. Repairs the methylated nucleobase in DNA by stoichiometrically
CC transferring the methyl group to a cysteine residue in the enzyme. This
CC is a suicide reaction: the enzyme is irreversibly inactivated.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein]
CC = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a
CC thymidine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:53428, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, ChEBI:CHEBI:137387;
CC EC=2.1.1.63; Evidence={ECO:0000255|PROSITE-ProRule:PRU10017};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion.;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and therefore is
CC not strictly catalytic. According to one definition, an enzyme is a
CC biocatalyst that acts repeatedly and over many reaction cycles.
CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000305}.
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DR EMBL; X54228; CAA38137.1; -; mRNA.
DR EMBL; M29971; AAA59596.1; -; mRNA.
DR EMBL; M31767; AAA52317.1; -; mRNA.
DR EMBL; M60761; AAA59594.1; -; mRNA.
DR EMBL; BT006714; AAP35360.1; -; mRNA.
DR EMBL; AL157832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49166.1; -; Genomic_DNA.
DR EMBL; BC000824; AAH00824.1; -; mRNA.
DR CCDS; CCDS7660.2; -.
DR PIR; A34889; XUHUMC.
DR RefSeq; NP_002403.2; NM_002412.4.
DR RefSeq; XP_005252739.1; XM_005252682.2.
DR PDB; 1EH6; X-ray; 2.00 A; A=1-207.
DR PDB; 1EH7; X-ray; 2.00 A; A=1-207.
DR PDB; 1EH8; X-ray; 2.50 A; A=1-207.
DR PDB; 1QNT; X-ray; 1.90 A; A=1-176.
DR PDB; 1T38; X-ray; 3.20 A; A=1-176.
DR PDB; 1T39; X-ray; 3.30 A; A/B=1-176.
DR PDB; 1YFH; X-ray; 3.01 A; A/B/C=1-179.
DR PDBsum; 1EH6; -.
DR PDBsum; 1EH7; -.
DR PDBsum; 1EH8; -.
DR PDBsum; 1QNT; -.
DR PDBsum; 1T38; -.
DR PDBsum; 1T39; -.
DR PDBsum; 1YFH; -.
DR AlphaFoldDB; P16455; -.
DR SMR; P16455; -.
DR BioGRID; 110411; 79.
DR IntAct; P16455; 2.
DR MINT; P16455; -.
DR STRING; 9606.ENSP00000302111; -.
DR BindingDB; P16455; -.
DR ChEMBL; CHEMBL2864; -.
DR DrugBank; DB00151; Cysteine.
DR DrugBank; DB11831; Dinitrochlorobenzene.
DR DrugBank; DB04531; S-Benzylcysteine.
DR DrugBank; DB02216; S-Methylcysteine.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyConnect; 1505; 3 N-Linked glycans (1 site).
DR GlyGen; P16455; 2 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P16455; -.
DR PhosphoSitePlus; P16455; -.
DR BioMuta; MGMT; -.
DR DMDM; 127069; -.
DR EPD; P16455; -.
DR jPOST; P16455; -.
DR MassIVE; P16455; -.
DR MaxQB; P16455; -.
DR PaxDb; P16455; -.
DR PeptideAtlas; P16455; -.
DR PRIDE; P16455; -.
DR ProteomicsDB; 53365; -.
DR ABCD; P16455; 1 sequenced antibody.
DR Antibodypedia; 32507; 898 antibodies from 42 providers.
DR CPTC; P16455; 1 antibody.
DR DNASU; 4255; -.
DR Ensembl; ENST00000651593.1; ENSP00000498729.1; ENSG00000170430.10.
DR GeneID; 4255; -.
DR KEGG; hsa:4255; -.
DR MANE-Select; ENST00000651593.1; ENSP00000498729.1; NM_002412.5; NP_002403.3.
DR UCSC; uc001lkh.3; human.
DR CTD; 4255; -.
DR DisGeNET; 4255; -.
DR GeneCards; MGMT; -.
DR HGNC; HGNC:7059; MGMT.
DR HPA; ENSG00000170430; Tissue enhanced (liver).
DR MalaCards; MGMT; -.
DR MIM; 156569; gene.
DR neXtProt; NX_P16455; -.
DR OpenTargets; ENSG00000170430; -.
DR Orphanet; 618; Familial melanoma.
DR Orphanet; 251579; Giant cell glioblastoma.
DR Orphanet; 251576; Gliosarcoma.
DR VEuPathDB; HostDB:ENSG00000170430; -.
DR eggNOG; KOG4062; Eukaryota.
DR GeneTree; ENSGT00390000015799; -.
DR HOGENOM; CLU_000445_52_2_1; -.
DR InParanoid; P16455; -.
DR PhylomeDB; P16455; -.
DR TreeFam; TF314064; -.
DR BRENDA; 2.1.1.63; 2681.
DR PathwayCommons; P16455; -.
DR Reactome; R-HSA-5657655; MGMT-mediated DNA damage reversal.
DR SignaLink; P16455; -.
DR SIGNOR; P16455; -.
DR BioGRID-ORCS; 4255; 7 hits in 1076 CRISPR screens.
DR ChiTaRS; MGMT; human.
DR EvolutionaryTrace; P16455; -.
DR GeneWiki; O-6-methylguanine-DNA_methyltransferase; -.
DR GenomeRNAi; 4255; -.
DR Pharos; P16455; Tchem.
DR PRO; PR:P16455; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P16455; protein.
DR Bgee; ENSG00000170430; Expressed in right lobe of liver and 176 other tissues.
DR ExpressionAtlas; P16455; baseline and differential.
DR Genevisible; P16455; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0009008; F:DNA-methyltransferase activity; TAS:ProtInc.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; TAS:ProtInc.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:Ensembl.
DR GO; GO:0006266; P:DNA ligation; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0060644; P:mammary gland epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:BHF-UCL.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IDA:BHF-UCL.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR CDD; cd06445; ATase; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR InterPro; IPR008332; MethylG_MeTrfase_N.
DR InterPro; IPR036631; MGMT_N_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01035; DNA_binding_1; 1.
DR Pfam; PF02870; Methyltransf_1N; 1.
DR SUPFAM; SSF46767; SSF46767; 1.
DR SUPFAM; SSF53155; SSF53155; 1.
DR TIGRFAMs; TIGR00589; ogt; 1.
DR PROSITE; PS00374; MGMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..207
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139359"
FT ACT_SITE 145
FT /note="Nucleophile; methyl group acceptor"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 95
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:15964013"
FT BINDING 114
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:15964013"
FT BINDING 115
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:15964013"
FT BINDING 123
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:15964013"
FT BINDING 128
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:15964013"
FT BINDING 151
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:15964013"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 30
FT /note="E -> K (in dbSNP:rs2020893)"
FT /id="VAR_014750"
FT VARIANT 53
FT /note="L -> F (in dbSNP:rs12917)"
FT /id="VAR_056129"
FT VARIANT 58
FT /note="P -> S (in dbSNP:rs2308322)"
FT /id="VAR_029112"
FT VARIANT 65
FT /note="W -> C (in dbSNP:rs2282164)"
FT /id="VAR_020354"
FT VARIANT 84
FT /note="L -> F (in dbSNP:rs12917)"
FT /id="VAR_014751"
FT VARIANT 112
FT /note="I -> V (in dbSNP:rs2308321)"
FT /id="VAR_056130"
FT VARIANT 143
FT /note="I -> V (in dbSNP:rs2308321)"
FT /id="VAR_014752"
FT VARIANT 160
FT /note="G -> R (in dbSNP:rs2308318)"
FT /id="VAR_014753"
FT VARIANT 166
FT /note="E -> D (in dbSNP:rs2308320)"
FT /id="VAR_014754"
FT VARIANT 178
FT /note="K -> R (in dbSNP:rs2308327)"
FT /id="VAR_014755"
FT MUTAGEN 114
FT /note="Y->A: Decreases activity towards methylated DNA over
FT 1000-fold. Slightly reduced reactivity with O6-
FT benzylguanine."
FT /evidence="ECO:0000269|PubMed:7766621"
FT MUTAGEN 114
FT /note="Y->E: Loss of DNA repair activity. Slightly reduced
FT reactivity with O6-benzylguanine."
FT /evidence="ECO:0000269|PubMed:7766621"
FT MUTAGEN 128
FT /note="R->A,D: Decreases activity towards methylated DNA
FT over 1000-fold. No effect on reactivity with O6-
FT benzylguanine."
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:7766621"
FT MUTAGEN 128
FT /note="R->G: Loss of DNA repair activity."
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:7766621"
FT MUTAGEN 128
FT /note="R->K,L: Slightly reduced DNA repair activity."
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:7766621"
FT MUTAGEN 138
FT /note="P->K: Decreased reactivity with O6-benzylguanine."
FT /evidence="ECO:0000269|PubMed:7954470"
FT MUTAGEN 140
FT /note="P->A: Decreased reactivity with O6-benzylguanine."
FT /evidence="ECO:0000269|PubMed:7954470"
FT MUTAGEN 145
FT /note="C->A: Loss of DNA repair activity."
FT /evidence="ECO:0000269|PubMed:10747039,
FT ECO:0000269|PubMed:7766621"
FT MUTAGEN 156
FT /note="G->A: Decreased reactivity with O6-benzylguanine."
FT /evidence="ECO:0000269|PubMed:7954470"
FT MUTAGEN 158
FT /note="Y->A: Reduced DNA repair activity. Decreased
FT reactivity with O6-benzylguanine."
FT /evidence="ECO:0000269|PubMed:7614699"
FT MUTAGEN 158
FT /note="Y->F: Slightly reduced DNA repair activity."
FT /evidence="ECO:0000269|PubMed:7614699"
FT CONFLICT 127
FT /note="A -> T (in Ref. 2; AAA52317)"
FT /evidence="ECO:0000305"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:1QNT"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1QNT"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1QNT"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1EH6"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:1QNT"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:1QNT"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1QNT"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:1QNT"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:1QNT"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1T38"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:1QNT"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1QNT"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1QNT"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:1QNT"
SQ SEQUENCE 207 AA; 21646 MW; 76BBF19DFC4512D6 CRC64;
MDKDCEMKRT TLDSPLGKLE LSGCEQGLHE IKLLGKGTSA ADAVEVPAPA AVLGGPEPLM
QCTAWLNAYF HQPEAIEEFP VPALHHPVFQ QESFTRQVLW KLLKVVKFGE VISYQQLAAL
AGNPKAARAV GGAMRGNPVP ILIPCHRVVC SSGAVGNYSG GLAVKEWLLA HEGHRLGKPG
LGGSSGLAGA WLKGAGATSG SPPAGRN
