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

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-3-methyladenine glycosylase

EC=3.2.2.21
Alternative name(s):
3-alkyladenine DNA glycosylase
3-methyladenine DNA glycosidase
ADPG
N-methylpurine-DNA glycosylase
Gene names
Name:MPG
Synonyms:AAG, ANPG, MID1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence 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. HAMAP-Rule MF_00527

Catalytic activity

Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine. HAMAP-Rule MF_00527

Subunit structure

Binds MBD1.

Subcellular location

Nucleus Potential HAMAP-Rule MF_00527.

Sequence similarities

Belongs to the DNA glycosylase MPG family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRNPP041564EBI-1043398,EBI-977302

Alternative products

This entry describes 4 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
Isoform 3 (identifier: P29372-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MVTPALQMKKPK → MPARSGA
Isoform 4 (identifier: P29372-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298DNA-3-methyladenine glycosylase HAMAP-Rule MF_00527
PRO_0000100065

Amino acid modifications

Modified residue781Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 1717Missing in isoform 4.
VSP_046678
Alternative sequence1 – 1212MVTPA…MKKPK → MPARSGA in isoform 2 and isoform 3.
VSP_003249
Alternative sequence195 – 1962QL → HV in isoform 2.
VSP_035485
Natural variant221K → Q. Ref.4
Corresponds to variant rs3176383 [ dbSNP | Ensembl ].
VAR_019138
Natural variant641P → L.
Corresponds to variant rs2308315 [ dbSNP | Ensembl ].
VAR_014831
Natural variant711Y → H. Ref.4
Corresponds to variant rs2266607 [ dbSNP | Ensembl ].
VAR_014832
Natural variant931Q → R.
Corresponds to variant rs25671 [ dbSNP | Ensembl ].
VAR_050096
Natural variant1201R → C.
Corresponds to variant rs2308313 [ dbSNP | Ensembl ].
VAR_014833
Natural variant1411R → Q.
Corresponds to variant rs2308312 [ dbSNP | Ensembl ].
VAR_014834
Natural variant2581A → V. Ref.4
Corresponds to variant rs769193 [ dbSNP | Ensembl ].
VAR_014835
Natural variant2981A → S. Ref.4
Corresponds to variant rs2234949 [ dbSNP | Ensembl ].
VAR_014836

Experimental info

Sequence conflict131Q → QV in AAK61213. Ref.5
Sequence conflict29 – 313GQP → ARA in AAB19537. Ref.9
Sequence conflict441Q → R in AAB19537. Ref.9
Sequence conflict69 – 713GPY → SKD in AAA58369. Ref.10
Sequence conflict69 – 713GPY → SKD in CAA39875. Ref.10
Sequence conflict821H → L in AAA58369. Ref.10
Sequence conflict821H → L in CAA39875. Ref.10
Sequence conflict1341A → P in AAA58627. Ref.1
Sequence conflict2871V → E in AAA58369. Ref.10

Secondary structure

............................................. 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 23, 2008. Version 3.
Checksum: BEA8C4CB250D572B

FASTA29832,869
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 81BE31859298D43C
Show »

FASTA29332,181
Isoform 3 [UniParc].

Checksum: 6F710D76409B2D81
Show »

FASTA29332,186
Isoform 4 [UniParc].

Checksum: 6826A6C692AABA9C
Show »

FASTA28130,824

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Identification of a human cell proliferation gene 11."
Kim J.W.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]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.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Pancreas.
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-298 (ISOFORMS 1/2).
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-298 (ISOFORMS 1/2).
[11]"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.F., Smits R., Devi T.S., Fodde R., Bernini L.F.
Mamm. Genome 4:314-323(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 230-298 (ISOFORMS 1/2).
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MBD1.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 80-199.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74905 mRNA. Translation: AAA58627.1.
L10752 mRNA. Translation: AAF77073.1.
AY258284 mRNA. Translation: AAP82229.1.
AY305873 mRNA. Translation: AAQ95215.1.
AF499437 Genomic DNA. Translation: AAM14628.1.
AE006462 Genomic DNA. Translation: AAK61213.1.
Z69720 Genomic DNA. Translation: CAA93540.1.
Z69720 Genomic DNA. Translation: CAI95610.1.
CH471112 Genomic DNA. Translation: EAW85871.1.
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.
PIRA40798.
A41230.
A47471.
JN0062.
RefSeqNP_001015052.1. NM_001015052.2.
NP_001015054.1. NM_001015054.2.
NP_002425.2. NM_002434.3.
UniGeneHs.459596.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BNKX-ray2.70A80-295[»]
1EWNX-ray2.10A80-298[»]
1F4RX-ray2.40A80-298[»]
1F6OX-ray2.40A80-298[»]
3QI5X-ray2.20A/B84-298[»]
3UBYX-ray2.00A/B84-298[»]
ProteinModelPortalP29372.
SMRP29372. Positions 82-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110490. 53 interactions.
IntActP29372. 3 interactions.
MINTMINT-135511.
STRING9606.ENSP00000219431.

PTM databases

PhosphoSiteP29372.

Proteomic databases

PaxDbP29372.
PRIDEP29372.

Protocols and materials databases

DNASU4350.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219431; ENSP00000219431; ENSG00000103152. [P29372-1]
ENST00000356432; ENSP00000348809; ENSG00000103152. [P29372-4]
ENST00000397817; ENSP00000380918; ENSG00000103152. [P29372-5]
GeneID4350.
KEGGhsa:4350.
UCSCuc002cfm.4. human. [P29372-1]
uc002cfo.4. human.

Organism-specific databases

CTD4350.
GeneCardsGC16P000127.
HGNCHGNC:7211. MPG.
HPAHPA006531.
MIM156565. gene.
neXtProtNX_P29372.
PharmGKBPA30917.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2094.
HOGENOMHOG000224224.
HOVERGENHBG000019.
InParanoidP29372.
KOK03652.
OMAEHISSQY.
PhylomeDBP29372.
TreeFamTF331768.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP29372.
BgeeP29372.
CleanExHS_MID1.
HS_MPG.
GenevestigatorP29372.

Family and domain databases

Gene3D3.10.300.10. 1 hit.
HAMAPMF_00527. 3MGH.
InterProIPR011034. Formyl_transferase_C-like.
IPR003180. PurDNA_glycsylse.
[Graphical view]
PANTHERPTHR10429. PTHR10429. 1 hit.
PfamPF02245. Pur_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMSSF50486. SSF50486. 1 hit.
TIGRFAMsTIGR00567. 3mg. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMPG. human.
EvolutionaryTraceP29372.
GeneWikiMPG_(gene).
GenomeRNAi4350.
NextBio17110.
PROP29372.
SOURCESearch...

Entry information

Entry name3MG_HUMAN
AccessionPrimary (citable) accession number: P29372
Secondary accession number(s): G5E9E2 expand/collapse secondary AC list , Q13770, Q15275, Q15961, Q5J9I4, Q96BZ6, Q96S33, Q9NNX5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM