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DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-alkyladenine DNA glycosylase) (3-methyladenine DNA glycosidase) (ADPG) (N-methylpurine-DNA glycosylase)

 3MG_HUMAN               Reviewed;         298 AA.
P29372; G5E9E2; Q13770; Q15275; Q15961; Q5J9I4; Q96BZ6; Q96S33;
Q9NNX5;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 3.
05-DEC-2018, entry version 202.
RecName: Full=DNA-3-methyladenine glycosylase;
EC=3.2.2.21;
AltName: Full=3-alkyladenine DNA glycosylase;
AltName: Full=3-methyladenine DNA glycosidase;
AltName: Full=ADPG;
AltName: Full=N-methylpurine-DNA glycosylase;
Flags: Precursor;
Name=MPG; Synonyms=AAG, ANPG, MID1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=1924375; DOI=10.1073/pnas.88.20.9127;
Samson L., Derfler B., Boosalis M., Call K.;
"Cloning and characterization of a 3-methyladenine DNA glycosylase
cDNA from human cells whose gene maps to chromosome 16.";
Proc. Natl. Acad. Sci. U.S.A. 88:9127-9131(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8475094; DOI=10.1073/pnas.90.8.3437;
Vickers M.A., Vyas P., Harris P.C., Simmons D.L., Higgs D.R.;
"Structure of the human 3-methyladenine DNA glycosylase gene and
localization close to the 16p telomere.";
Proc. Natl. Acad. Sci. U.S.A. 90:3437-3441(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Kim J.W.;
"Identification of a human cell proliferation gene 11.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-22; HIS-71;
VAL-258 AND SER-298.
NIEHS SNPs program;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-298 (ISOFORMS 1/2).
PubMed=1874728;
Chakravarti D., Ibeanu G.C., Tano K., Mitra S.;
"Cloning and expression in Escherichia coli of a human cDNA encoding
the DNA repair protein N-methylpurine-DNA glycosylase.";
J. Biol. Chem. 266:15710-15715(1991).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 69-298 (ISOFORMS 1/2).
PubMed=1645538; DOI=10.1016/0006-291X(91)90408-Y;
O'Connor T.R., Laval J.;
"Human cDNA expressing a functional DNA glycosylase excising 3-
methyladenine and 7-methylguanine.";
Biochem. Biophys. Res. Commun. 176:1170-1177(1991).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 230-298 (ISOFORMS 1/2).
PubMed=8318735; DOI=10.1007/BF00357090;
Kielman M.F., Smits R., Devi T.S., Fodde R., Bernini L.F.;
"Homology of a 130-kb region enclosing the alpha-globin gene cluster,
the alpha-locus controlling region, and two non-globin genes in human
and mouse.";
Mamm. Genome 4:314-323(1993).
[12]
INTERACTION WITH MBD1.
PubMed=14555760; DOI=10.1073/pnas.2131819100;
Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I.,
Shirakawa M., Kawasuji M., Nakao M.;
"Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link
transcriptional repression and DNA repair in chromatin.";
Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
SUBCELLULAR LOCATION, INTERACTION WITH SSBP1, AND ACTIVITY REGULATION.
PubMed=23290262; DOI=10.1016/j.dnarep.2012.11.009;
van Loon B., Samson L.D.;
"Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and
interacts with mitochondrial single-stranded binding protein
(mtSSB).";
DNA Repair 12:177-187(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 80-199.
PubMed=9790531; DOI=10.1016/S0092-8674(00)81755-9;
Lau A.Y., Scharer O.D., Samson L., Verdine G.L., Ellenberger T.;
"Crystal structure of a human alkylbase-DNA repair enzyme complexed to
DNA: mechanisms for nucleotide flipping and base excision.";
Cell 95:249-258(1998).
-!- 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:
Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine,
3-methylguanine, 7-methylguanine and 7-methyladenine.;
EC=3.2.2.21;
-!- ACTIVITY REGULATION: Binding to SSBP1 in mitochondria inhibits
glycosylase activity in the context of a single-stranded DNA
(ssDNA), but not a double-stranded DNA (dsDNA) substrates.
{ECO:0000269|PubMed:23290262}.
-!- SUBUNIT: Binds MBD1. Binds SSBP1.
-!- INTERACTION:
Q9BPX1:HSD17B14; NbExp=3; IntAct=EBI-1043398, EBI-742664;
P04156:PRNP; NbExp=4; IntAct=EBI-1043398, EBI-977302;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23290262}.
Mitochondrion matrix, mitochondrion nucleoid
{ECO:0000269|PubMed:23290262}. Nucleus
{ECO:0000269|PubMed:23290262}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=P29372-1; Sequence=Displayed;
Name=2;
IsoId=P29372-2; Sequence=VSP_003249, VSP_035485;
Name=3;
IsoId=P29372-4; Sequence=VSP_003249;
Name=4;
IsoId=P29372-5; Sequence=VSP_046678;
Note=Gene prediction based on EST data.;
-!- SIMILARITY: Belongs to the DNA glycosylase MPG family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mpg/";
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EMBL; M74905; AAA58627.1; -; mRNA.
EMBL; L10752; AAF77073.1; -; mRNA.
EMBL; AY258284; AAP82229.1; -; mRNA.
EMBL; AY305873; AAQ95215.1; -; mRNA.
EMBL; AF499437; AAM14628.1; -; Genomic_DNA.
EMBL; AE006462; AAK61213.1; -; Genomic_DNA.
EMBL; Z69720; CAA93540.1; -; Genomic_DNA.
EMBL; Z69720; CAI95610.1; -; Genomic_DNA.
EMBL; CH471112; EAW85871.1; -; Genomic_DNA.
EMBL; BC014991; AAH14991.1; -; mRNA.
EMBL; S51033; AAB19537.1; -; mRNA.
EMBL; X56528; CAA39875.1; -; mRNA.
EMBL; M71215; AAA58369.1; -; mRNA.
EMBL; M99626; AAB46421.1; -; mRNA.
CCDS; CCDS32345.1; -. [P29372-4]
CCDS; CCDS32346.1; -. [P29372-1]
CCDS; CCDS42087.1; -. [P29372-5]
PIR; A40798; A40798.
PIR; A41230; A41230.
PIR; A47471; A47471.
PIR; JN0062; JN0062.
RefSeq; NP_001015052.1; NM_001015052.2. [P29372-4]
RefSeq; NP_001015054.1; NM_001015054.2. [P29372-5]
RefSeq; NP_002425.2; NM_002434.3. [P29372-1]
UniGene; Hs.459596; -.
PDB; 1BNK; X-ray; 2.70 A; A=80-295.
PDB; 1EWN; X-ray; 2.10 A; A=80-298.
PDB; 1F4R; X-ray; 2.40 A; A=80-298.
PDB; 1F6O; X-ray; 2.40 A; A=80-298.
PDB; 3QI5; X-ray; 2.20 A; A/B=84-298.
PDB; 3UBY; X-ray; 2.00 A; A/B=84-298.
PDBsum; 1BNK; -.
PDBsum; 1EWN; -.
PDBsum; 1F4R; -.
PDBsum; 1F6O; -.
PDBsum; 3QI5; -.
PDBsum; 3UBY; -.
ProteinModelPortal; P29372; -.
SMR; P29372; -.
BioGrid; 110490; 71.
IntAct; P29372; 15.
MINT; P29372; -.
STRING; 9606.ENSP00000219431; -.
BindingDB; P29372; -.
ChEMBL; CHEMBL3396943; -.
iPTMnet; P29372; -.
PhosphoSitePlus; P29372; -.
BioMuta; MPG; -.
EPD; P29372; -.
PaxDb; P29372; -.
PeptideAtlas; P29372; -.
PRIDE; P29372; -.
ProteomicsDB; 54553; -.
ProteomicsDB; 54554; -. [P29372-2]
TopDownProteomics; P29372-1; -. [P29372-1]
DNASU; 4350; -.
Ensembl; ENST00000219431; ENSP00000219431; ENSG00000103152. [P29372-1]
Ensembl; ENST00000356432; ENSP00000348809; ENSG00000103152. [P29372-4]
Ensembl; ENST00000397817; ENSP00000380918; ENSG00000103152. [P29372-5]
GeneID; 4350; -.
KEGG; hsa:4350; -.
UCSC; uc002cfm.4; human. [P29372-1]
CTD; 4350; -.
DisGeNET; 4350; -.
EuPathDB; HostDB:ENSG00000103152.11; -.
GeneCards; MPG; -.
HGNC; HGNC:7211; MPG.
HPA; HPA006531; -.
MIM; 156565; gene.
neXtProt; NX_P29372; -.
OpenTargets; ENSG00000103152; -.
PharmGKB; PA30917; -.
eggNOG; KOG4486; Eukaryota.
eggNOG; COG2094; LUCA.
GeneTree; ENSGT00390000009825; -.
HOGENOM; HOG000224224; -.
HOVERGEN; HBG000019; -.
InParanoid; P29372; -.
KO; K03652; -.
OMA; VEAYHHT; -.
OrthoDB; EOG091G0NE4; -.
PhylomeDB; P29372; -.
TreeFam; TF331768; -.
BRENDA; 3.2.2.21; 2681.
Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
Reactome; R-HSA-110331; Cleavage of the damaged purine.
Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
SABIO-RK; P29372; -.
ChiTaRS; MPG; human.
EvolutionaryTrace; P29372; -.
GeneWiki; MPG_(gene); -.
GenomeRNAi; 4350; -.
PRO; PR:P29372; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103152; Expressed in 222 organ(s), highest expression level in tibial artery.
CleanEx; HS_MID1; -.
CleanEx; HS_MPG; -.
ExpressionAtlas; P29372; baseline and differential.
Genevisible; P29372; HS.
GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; IBA:GO_Central.
GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
GO; GO:0019104; F:DNA N-glycosylase activity; TAS:Reactome.
GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:UniProtKB-EC.
GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IEA:UniProtKB-EC.
GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
GO; GO:0045007; P:depurination; TAS:Reactome.
GO; GO:0006307; P:DNA dealkylation involved in DNA repair; TAS:ProtInc.
CDD; cd00540; AAG; 1.
Gene3D; 3.10.300.10; -; 1.
HAMAP; MF_00527; 3MGH; 1.
InterPro; IPR011034; Formyl_transferase-like_C_sf.
InterPro; IPR003180; MPG.
InterPro; IPR036995; MPG_sf.
PANTHER; PTHR10429; PTHR10429; 1.
Pfam; PF02245; Pur_DNA_glyco; 1.
SUPFAM; SSF50486; SSF50486; 1.
TIGRFAMs; TIGR00567; 3mg; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
DNA damage; DNA repair; Hydrolase; Mitochondrion;
Mitochondrion nucleoid; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transit peptide.
TRANSIT 1 17 Mitochondrion. {ECO:0000255}.
CHAIN 18 298 DNA-3-methyladenine glycosylase.
/FTId=PRO_0000100065.
MOD_RES 78 78 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 17 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_046678.
VAR_SEQ 1 12 MVTPALQMKKPK -> MPARSGA (in isoform 2 and
isoform 3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8475094,
ECO:0000303|Ref.3}.
/FTId=VSP_003249.
VAR_SEQ 195 196 QL -> HV (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8475094}.
/FTId=VSP_035485.
VARIANT 22 22 K -> Q (in dbSNP:rs3176383).
{ECO:0000269|Ref.4}.
/FTId=VAR_019138.
VARIANT 64 64 P -> L (in dbSNP:rs2308315).
/FTId=VAR_014831.
VARIANT 71 71 Y -> H (in dbSNP:rs2266607).
{ECO:0000269|Ref.4}.
/FTId=VAR_014832.
VARIANT 93 93 Q -> R (in dbSNP:rs25671).
/FTId=VAR_050096.
VARIANT 120 120 R -> C (in dbSNP:rs2308313).
/FTId=VAR_014833.
VARIANT 141 141 R -> Q (in dbSNP:rs2308312).
/FTId=VAR_014834.
VARIANT 258 258 A -> V (in dbSNP:rs769193).
{ECO:0000269|Ref.4}.
/FTId=VAR_014835.
VARIANT 298 298 A -> S (in dbSNP:rs2234949).
{ECO:0000269|Ref.4}.
/FTId=VAR_014836.
CONFLICT 13 13 Q -> QV (in Ref. 5; AAK61213).
{ECO:0000305}.
CONFLICT 29 31 GQP -> ARA (in Ref. 9; AAB19537).
{ECO:0000305}.
CONFLICT 44 44 Q -> R (in Ref. 9; AAB19537).
{ECO:0000305}.
CONFLICT 69 71 GPY -> SKD (in Ref. 10; AAA58369/
CAA39875). {ECO:0000305}.
CONFLICT 82 82 H -> L (in Ref. 10; AAA58369/CAA39875).
{ECO:0000305}.
CONFLICT 134 134 A -> P (in Ref. 1; AAA58627).
{ECO:0000305}.
CONFLICT 287 287 V -> E (in Ref. 10; AAA58369).
{ECO:0000305}.
HELIX 82 84 {ECO:0000244|PDB:1F6O}.
HELIX 88 91 {ECO:0000244|PDB:3UBY}.
HELIX 95 101 {ECO:0000244|PDB:3UBY}.
TURN 102 104 {ECO:0000244|PDB:3UBY}.
STRAND 106 110 {ECO:0000244|PDB:3UBY}.
STRAND 116 127 {ECO:0000244|PDB:3UBY}.
STRAND 129 131 {ECO:0000244|PDB:1F6O}.
HELIX 138 140 {ECO:0000244|PDB:3UBY}.
HELIX 145 150 {ECO:0000244|PDB:3UBY}.
STRAND 155 161 {ECO:0000244|PDB:3UBY}.
TURN 162 164 {ECO:0000244|PDB:3UBY}.
STRAND 165 171 {ECO:0000244|PDB:3UBY}.
STRAND 178 188 {ECO:0000244|PDB:3UBY}.
HELIX 190 199 {ECO:0000244|PDB:3UBY}.
HELIX 211 213 {ECO:0000244|PDB:3UBY}.
STRAND 214 217 {ECO:0000244|PDB:3UBY}.
HELIX 218 224 {ECO:0000244|PDB:3UBY}.
HELIX 229 231 {ECO:0000244|PDB:3UBY}.
TURN 236 238 {ECO:0000244|PDB:3UBY}.
STRAND 240 245 {ECO:0000244|PDB:3UBY}.
HELIX 253 255 {ECO:0000244|PDB:3UBY}.
STRAND 256 259 {ECO:0000244|PDB:3UBY}.
TURN 268 272 {ECO:0000244|PDB:3UBY}.
STRAND 276 279 {ECO:0000244|PDB:3UBY}.
TURN 290 292 {ECO:0000244|PDB:3UBY}.
SEQUENCE 298 AA; 32869 MW; BEA8C4CB250D572B CRC64;
MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD AAQAPCPRER
CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR AFLGQVLVRR LPNGTELRGR
IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYI IYGMYFCMNI SSQGDGACVL
LRALEPLEGL ETMRQLRSTL RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE
AVWLERGPLE PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQA


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E97625Hu ELISA Kit for N-Methylpurine DNA Glycosylase (MPG) 96T/Kit
DL-MPG-Hu Human N-Methylpurine DNA Glycosylase (MPG) ELISA Kit 96T
201-20-3440 MPG{N-methylpurine-DNA glycosylase}rabbit.pAb 0.2ml
enz-151 Recombinant Human N-Methylpurine-DNA Glycosylase 10
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MPHOSPH6 MPG Gene N-methylpurine-DNA glycosylase
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REN-151 Recombinant Human N-Methylpurine-DNA Glycosylase 1mg
enz-151 Recombinant Human N-Methylpurine-DNA Glycosylase ENZYMES 10
E13651316 Human N-Methylpurine DNA Glycosylase (MPG) ELISA Kit 1


 

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