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Description:
DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-methyladenine DNAglycosidase) (ADPG) (3-alkyladenine DNA glycosylase) (N-methylpurine-DNA glycosirase).
Molecular weight: 32864
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) base-excision repair( GO:0006284 ) DNA dealkylation( GO:0006307 )
Important dates:
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
07-FEB-2006, entry version 63.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein 3MG_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M74905 | AAA58627.1 | - |
| EMBL | L10752 | AAF77073.1 | - |
| EMBL | AE006462 | AAK61213.1 | - |
| EMBL | AF499437 | AAM14628.1 | - |
| EMBL | Z69720 | CAA93540.1 | - |
| EMBL | BC014991 | AAH14991.1 | - |
| EMBL | S51033 | AAB19537.1 | - |
| EMBL | X56528 | CAA39875.1 | - |
| EMBL | M71215 | AAA58369.1 | - |
| EMBL | M99626 | AAB46421.1 | - |
| PIR | A40798 | A40798. | |
| PIR | A41230 | A41230. | |
| PIR | A47471 | A47471. | |
| PIR | JN0062 | JN0062. | |
| PDB | 1BNK | X-ray | A=80-295. |
| PDB | 1EWN | X-ray | A=80-298. |
| PDB | 1F4R | X-ray | A=80-298. |
| PDB | 1F6O | X-ray | A=80-298. |
| Ensembl | ENSG00000103152 | Homo sapiens.1 | |
| H-InvDB | HIX0012638 | -.1 | |
| HGNC | HGNC:7211 | MPG.1 | |
| MIM | 156565 | gene. | |
| Reactome | P29372 | -.1 | |
| GO | GO:0005654 | C:nucleoplasm | TAS. |
| GO | GO:0003684 | F:damaged DNA binding | TAS. |
| GO | GO:0006284 | P:base-excision repair | TAS. |
| GO | GO:0006307 | P:DNA dealkylation | TAS. |
| InterPro | IPR003180 | PurDNA_glycsylse. | |
| PANTHER | PTHR10429 | PurDNA_glycsylse.1 | 1. |
| Pfam | PF02245 | Pur_DNA_glyco | 1. |
| ProDom | PD009649 | PurDNA_glycsylse | 1. |
| TIGRFAMs | TIGR00567 | 3mg | 1. |
Keywords:
3D-structure; Alternative splicing; DNA damage; DNA repair; Hydrolase; Nuclear protein; Phosphorylation; Polymorphism.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX MEDLINE=92021003; PubMed=1924375;
RA Samson L., Derfler B., Boosalis M., Call K.;
RT "Cloning and characterization of a 3-methyladenine DNA glycosylase
RT cDNA from human cells whose gene maps to chromosome 16.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9127-9131(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RX MEDLINE=93234512; PubMed=8475094;
RA Vickers M.A., Vyas P., Harris P.C., Simmons D.L., Higgs D.R.;
RT "Structure of the human 3-methyladenine DNA glycosylase gene and
RT localization close to the 16p telomere.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3437-3441(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=21096910; PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2
RT Mb of the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-22; HIS-71;
RP VAL-258 AND SER-298.
RA Rieder M.J., Braun A.C., Montoya M.A., Chung M.-W., Nguyen C.P.,
RA Nguyen D.A., Livingston R.J., Poel C.L., Robertson P.D.,
RA Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE OF 28-298.
RX MEDLINE=91340707; PubMed=1874728;
RA Chakravarti D., Ibeanu G.C., Tano K., Mitra S.;
RT "Cloning and expression in Escherichia coli of a human cDNA encoding
RT the DNA repair protein N-methylpurine-DNA glycosylase.";
RL J. Biol. Chem. 266:15710-15715(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE OF 69-298.
RX MEDLINE=91248199; PubMed=1645538;
RA O'Connor T.R., Laval J.;
RT "Human cDNA expressing a functional DNA glycosylase excising 3-
RT methyladenine and 7-methylguanine.";
RL Biochem. Biophys. Res. Commun. 176:1170-1177(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE OF 230-298.
RX MEDLINE=93305988; PubMed=8318735;
RA Kielman M., Smits R., Devi T., Fodde R., Bernini L.F.;
RT "Homology of a 130-kb region enclosing the alpha-globin gene cluster,
RT the alpha-locus controlling region, and two non-globin genes in human
RT and mouse.";
RL Mamm. Genome 4:314-323(1993).
RN [10]
RP INTERACTION WITH MBD1.
RX PubMed=14555760; DOI=10.1073/pnas.2131819100;
RA Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I.,
RA Shirakawa M., Kawasuji M., Nakao M.;
RT "Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link
RT transcriptional repression and DNA repair in chromatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003).
RN [11]
RP PHOSPHORYLATION SITE SER-252.
RX PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 80-199.
RX MEDLINE=99005192; PubMed=9790531; DOI=10.1016/S0092-8674(00)81755-9;
RA Lau A.Y., Scharer O.D., Samson L., Verdine G.L., Ellenberger T.;
RT "Crystal structure of a human alkylbase-DNA repair enzyme complexed to
RT DNA: mechanisms for nucleotide flipping and base excision.";
RL Cell 95:249-258(1998).
Feature:
CHAIN 1 298 DNA-3-methyladenine glycosylase.
/FTId=PRO_0000100065.
MOD_RES 252 252 Phosphoserine.
VARSPLIC 1 12 MVTPALQMKKPK -> MPARSGA (in isoform 2).
/FTId=VSP_003249.
VARSPLIC 195 196 HV -> QL (in isoform 3).
/FTId=VSP_003250.
VARIANT 22 22 K -> Q.
/FTId=VAR_019138.
VARIANT 64 64 P -> L (in dbSNP:2308315).
/FTId=VAR_014831.
VARIANT 71 71 Y -> H (in dbSNP:769184).
/FTId=VAR_014832.
VARIANT 120 120 R -> C (in dbSNP:2308313).
/FTId=VAR_014833.
VARIANT 141 141 R -> Q (in dbSNP:2308312).
/FTId=VAR_014834.
VARIANT 258 258 A -> V (in dbSNP:769193).
/FTId=VAR_014835.
VARIANT 298 298 A -> S (in dbSNP:2234949).
/FTId=VAR_014836.
CONFLICT 13 13 Q -> QV (in Ref. 3).
CONFLICT 29 31 GQP -> ARA (in Ref. 7).
CONFLICT 44 44 Q -> R (in Ref. 7).
CONFLICT 69 71 GPY -> SKD (in Ref. 8).
CONFLICT 82 82 H -> L (in Ref. 8).
CONFLICT 134 134 A -> P (in Ref. 1).
CONFLICT 287 287 V -> E (in Ref. 8).
TURN 83 84
STRAND 85 85
HELIX 88 91
STRAND 93 94
HELIX 95 102
TURN 103 104
STRAND 106 110
TURN 112 113
STRAND 114 114
STRAND 116 127
STRAND 129 129
TURN 130 131
TURN 133 134
STRAND 135 135
TURN 136 137
HELIX 138 140
STRAND 144 146
HELIX 147 150
STRAND 151 152
TURN 153 154
STRAND 155 161
TURN 162 164
STRAND 165 171
STRAND 173 174
TURN 175 176
STRAND 178 188
HELIX 190 196
TURN 197 198
HELIX 211 213
STRAND 214 217
HELIX 218 224
TURN 225 226
HELIX 229 231
TURN 232 233
STRAND 235 235
TURN 236 237
STRAND 238 238
STRAND 240 245
STRAND 256 259
TURN 262 263
STRAND 266 266
STRAND 268 268
HELIX 269 272
STRAND 273 273
STRAND 276 279
TURN 280 281
TURN 283 284
STRAND 286 287
HELIX 290 293
TURN 294 294
Comments:
-!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to
excise 3-methyladenine, and 7-methylguanine from the damaged DNA
polymer formed by alkylation lesions.
-!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3-
methyladenine, 3-methylguanine, 7-methylguanine and 7-
methyladenine.
-!- SUBUNIT: Binds MBD1.
-!- SUBCELLULAR LOCATION: Nucleus (Potential).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Experimental confirmation may be lacking for some
isoforms;
Name=1;
IsoId=P29372-1; Sequence=Displayed;
Name=2;
IsoId=P29372-2; Sequence=VSP_003249;
Name=3;
IsoId=P29372-3; Sequence=VSP_003250;
-!- SIMILARITY: Belongs to the DNA glycosylase MPG family.
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Sequence length: 298
MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD AAQAPCPRER
CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR AFLGQVLVRR LPNGTELRGR
IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYI IYGMYFCMNI SSQGDGACVL
LRALEPLEGL ETMRHVRSTL RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE
AVWLERGPLE PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQA