Reviewed, UniProtKB/Swiss-Prot P29372 (3MG_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA-3-methyladenine glycosylase
    EC=3.2.2.21
Alternative name(s):
    3-methyladenine DNA glycosidase
    ADPG
    3-alkyladenine DNA glycosylase
    N-methylpurine-DNA glycosylase

Gene names

Name:	MPG
Synonyms:	AAG, ANPG, MID1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 structure	Binds MBD1.
Subcellular location	Nucleus Potential.
Sequence similarities	Belongs to the DNA glycosylase MPG family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA dealkylation Ref.8 Traceable author statement. Source: ProtInc depurination Inferred from Experiment. Source: Reactome
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	alkylbase DNA N-glycosylase activity Inferred from electronic annotation. Source: EC damaged DNA binding Traceable author statement. Source: ProtInc identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-1043398,EBI-1043398
FBLN1	P23142	1	EBI-1043398,EBI-726652
GSTM3	P21266	1	EBI-1043398,EBI-350350
LRRC59	Q96AG4	1	EBI-1043398,EBI-358888
RANBP1	P43487	1	EBI-1043398,EBI-1032909

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: P29372-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P29372-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MVTPALQMKKPK → MPARSGA
     195-196: QL → HV

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 298

298

DNA-3-methyladenine glycosylase

PRO_0000100065

Amino acid modifications

Modified residue

78

1

Phosphoserine Ref.12

Modified residue

252

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1 – 12

12

MVTPA…MKKPK → MPARSGA in isoform 2.

VSP_003249

Alternative sequence

195 – 196

2

QL → HV in isoform 2.

VSP_035485

Natural variant

22

1

K → Q: dbSNP rs3176383. Ref.3

VAR_019138

Natural variant

64

1

P → L: dbSNP rs2308315.

VAR_014831

Natural variant

71

1

Y → H: dbSNP rs2266607. Ref.3

VAR_014832

Natural variant

93

1

Q → R: dbSNP rs25671.

VAR_050096

Natural variant

120

1

R → C: dbSNP rs2308313.

VAR_014833

Natural variant

141

1

R → Q: dbSNP rs2308312.

VAR_014834

Natural variant

258

1

A → V: dbSNP rs769193. Ref.3

VAR_014835

Natural variant

298

1

A → S: dbSNP rs2234949. Ref.3

VAR_014836

Experimental info

Sequence conflict

13

1

Q → QV in AAK61213. Ref.4

Sequence conflict

29 – 31

3

GQP → ARA in AAB19537. Ref.7

Sequence conflict

44

1

Q → R in AAB19537. Ref.7

Sequence conflict

69 – 71

3

GPY → SKD in AAA58369. Ref.8

Sequence conflict

69 – 71

3

GPY → SKD in CAA39875. Ref.8

Sequence conflict

82

1

H → L in AAA58369. Ref.8

Sequence conflict

82

1

H → L in CAA39875. Ref.8

Sequence conflict

134

1

A → P in AAA58627. Ref.1

Sequence conflict

287

1

V → E in AAA58369. Ref.8

Secondary structure

1

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298

Helix Strand Turn

Details...

Helix

88 – 91

4

Helix

95 – 102

8

Beta strand

106 – 110

5

Beta strand

116 – 127

12

Helix

138 – 140

3

Beta strand

144 – 146

3

Helix

147 – 150

4

Beta strand

155 – 161

7

Turn

162 – 164

3

Beta strand

165 – 171

7

Beta strand

178 – 188

11

Helix

190 – 196

7

Helix

211 – 213

3

Beta strand

214 – 217

4

Helix

218 – 224

7

Helix

229 – 231

3

Beta strand

240 – 245

6

Beta strand

256 – 259

4

Helix

269 – 272

4

Beta strand

276 – 279

4

Helix

290 – 293

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 23, 2008. Version 3. Checksum: BEA8C4CB250D572B	FASTA	298	32,869
	10 20 30 40 50 60 MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD AAQAPCPRER 70 80 90 100 110 120 CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR AFLGQVLVRR LPNGTELRGR 130 140 150 160 170 180 IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYI IYGMYFCMNI SSQGDGACVL 190 200 210 220 230 240 LRALEPLEGL ETMRQLRSTL RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE 250 260 270 280 290 AVWLERGPLE PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQA
	Isoform 2. Checksum: 81BE31859298D43C	FASTA	293	32,181
	10 20 30 40 50 60 MPARSGAQFC RRMGQKKQRP ARAGQPHSSS DAAQAPAEQP HSSSDAAQAP CPRERCLGPP 70 80 90 100 110 120 TTPGPYRSIY FSSPKGHLTR LGLEFFDQPA VPLARAFLGQ VLVRRLPNGT ELRGRIVETE 130 140 150 160 170 180 AYLGPEDEAA HSRGGRQTPR NRGMFMKPGT LYVYIIYGMY FCMNISSQGD GACVLLRALE 190 200 210 220 230 240 PLEGLETMRH VRSTLRKGTA SRVLKDRELC SGPSKLCQAL AINKSFDQRD LAQDEAVWLE 250 260 270 280 290 RGPLEPSEPA VVAAARVGVG HAGEWARKPL RFYVRGSPWV SVVDRVAEQD TQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16." Samson L., Derfler B., Boosalis M., Call K. Proc. Natl. Acad. Sci. U.S.A. 88:9127-9131(1991) [PubMed: 1924375] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[2]	"Structure of the human 3-methyladenine DNA glycosylase gene and localization close to the 16p telomere." Vickers M.A., Vyas P., Harris P.C., Simmons D.L., Higgs D.R. Proc. Natl. Acad. Sci. U.S.A. 90:3437-3441(1993) [PubMed: 8475094] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	NIEHS SNPs program Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-22; HIS-71; VAL-258 AND SER-298.
[4]	"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16." 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. Hum. Mol. Genet. 10:339-352(2001) [PubMed: 11157797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The sequence and analysis of duplication-rich human chromosome 16." 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. Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Pancreas.
[7]	"Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase." Chakravarti D., Ibeanu G.C., Tano K., Mitra S. J. Biol. Chem. 266:15710-15715(1991) [PubMed: 1874728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-298 (ISOFORM 1/2).
[8]	"Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine." O'Connor T.R., Laval J. Biochem. Biophys. Res. Commun. 176:1170-1177(1991) [PubMed: 1645538] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-298 (ISOFORM 1/2).
[9]	"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." Kielman M., Smits R., Devi T., Fodde R., Bernini L.F. Mamm. Genome 4:314-323(1993) [PubMed: 8318735] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 230-298 (ISOFORM 1/2).
[10]	"Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin." Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., Shirakawa M., Kawasuji M., Nakao M. Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003) [PubMed: 14555760] [Abstract] Cited for: INTERACTION WITH MBD1.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, MASS SPECTROMETRY.
[13]	"Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision." Lau A.Y., Scharer O.D., Samson L., Verdine G.L., Ellenberger T. Cell 95:249-258(1998) [PubMed: 9790531] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 80-199.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M74905 mRNA. Translation: AAA58627.1.
L10752 mRNA. Translation: AAF77073.1.
AF499437 Genomic DNA. Translation: AAM14628.1.
AE006462 Genomic DNA. Translation: AAK61213.1.
Z69720 Genomic DNA. Translation: CAA93540.1.
BC014991 mRNA. Translation: AAH14991.1.
S51033 mRNA. Translation: AAB19537.1.
X56528 mRNA. Translation: CAA39875.1.
M71215 mRNA. Translation: AAA58369.1.
M99626 mRNA. Translation: AAB46421.1.

IPI

IPI00218495.
IPI00295497.

PIR

A40798.
A41230.
A47471.
JN0062.

RefSeq

NP_001015052.1.
NP_001015054.1.
NP_002425.2.

UniGene

Hs.459596

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BNK	X-ray	2.70	A	80-295	[»]
1EWN	X-ray	2.10	A	80-298	[»]
1F4R	X-ray	2.40	A	80-298	[»]
1F6O	X-ray	2.40	A	80-298	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P29372. 30 interactions.

PTM databases

PhosphoSite

P29372.

Genome annotation databases

Ensembl

ENSG00000103152. Homo sapiens. [Contig view]

GeneID

4350.

KEGG

hsa:4350.

Organism-specific databases

GeneCards

GC16P000068.

H-InvDB

HIX0012638.

HGNC

HGNC:7211. MPG.

HPA

HPA006531.

MIM

156565. gene.

PharmGKB

PA30917.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P29372.

OMA

P29372. YHCFNVI.

Enzyme and pathway databases

BRENDA

3.2.2.21. 247.

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

P29372.

Bgee

P29372.

CleanEx

HS_MID1.
HS_MPG.

GermOnline

ENSG00000103152. Homo sapiens.

Family and domain databases

InterPro

IPR003180. PurDNA_glycsylse.
[Graphical view]

Gene3D

G3DSA:3.10.300.10. PurDNA_glycsylse. 1 hit.

PANTHER

PTHR10429. PurDNA_glycsylse. 1 hit.

Pfam

PF02245. Pur_DNA_glyco. 1 hit.
[Graphical view]

ProDom

PD009649. PurDNA_glycsylse. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00567. 3mg. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

17110.

SOURCE

Search...

Entry information

Entry name

3MG_HUMAN

Accession

Primary (citable) accession number: P29372
Secondary accession number(s): Q13770 , Q15275, Q15961, Q96BZ6, Q96S33, Q9NNX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	September 23, 2008
Last modified:	June 16, 2009
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)