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   27-MAR-2024, entry version 217.
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; CCDS7660.3; -.
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; 84.
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   GlyCosmos; P16455; 2 sites, 4 glycans.
DR   GlyGen; P16455; 4 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (3 sites).
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; 9606-ENSP00000302111; -.
DR   PeptideAtlas; P16455; -.
DR   ProteomicsDB; 53365; -.
DR   Pumba; P16455; -.
DR   ABCD; P16455; 1 sequenced antibody.
DR   Antibodypedia; 32507; 1024 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   AGR; HGNC:7059; -.
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; 8 hits in 1162 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 178 other cell types or tissues.
DR   ExpressionAtlas; P16455; baseline and differential.
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:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0009008; F:DNA-methyltransferase activity; TAS:ProtInc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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: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   CDD; cd06445; ATase; 1.
DR   Gene3D; 3.30.160.70; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   NCBIfam; TIGR00589; ogt; 1.
DR   PANTHER; PTHR46460; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46460:SF1; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   Pfam; PF02870; Methyltransf_1N; 1.
DR   SUPFAM; SSF53155; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR   SUPFAM; SSF46767; Methylated DNA-protein cysteine methyltransferase, C-terminal domain; 1.
DR   PROSITE; PS00374; MGMT; 1.
DR   Genevisible; P16455; HS.
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
FT                   O6-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
FT                   O6-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
//