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Protein

DNA-3-methyladenine glycosylase

Gene

MPG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.

Catalytic activityi

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

Enzyme regulationi

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.1 Publication

GO - Molecular functioni

  1. alkylbase DNA N-glycosylase activity Source: GO_Central
  2. damaged DNA binding Source: ProtInc
  3. DNA-3-methyladenine glycosylase activity Source: UniProtKB-EC
  4. DNA-3-methylguanine glycosylase activity Source: UniProtKB-EC
  5. DNA-7-methyladenine glycosylase activity Source: UniProtKB-EC
  6. DNA-7-methylguanine glycosylase activity Source: UniProtKB-EC

GO - Biological processi

  1. base-excision repair Source: GO_Central
  2. base-excision repair, AP site formation Source: Reactome
  3. depurination Source: Reactome
  4. DNA dealkylation involved in DNA repair Source: ProtInc
  5. DNA repair Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BRENDAi3.2.2.21. 2681.
ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
REACT_1729. Cleavage of the damaged purine.
REACT_2176. Recognition and association of DNA glycosylase with site containing an affected purine.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MPG
Synonyms:AAG, ANPG, MID1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:7211. MPG.

Subcellular locationi

Cytoplasm 1 Publication. Mitochondrion matrixmitochondrion nucleoid 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. mitochondrial nucleoid Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Mitochondrion nucleoid, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30917.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717MitochondrionSequence AnalysisAdd
BLAST
Chaini18 – 298281DNA-3-methyladenine glycosylasePRO_0000100065Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29372.
PaxDbiP29372.
PRIDEiP29372.

PTM databases

PhosphoSiteiP29372.

Expressioni

Gene expression databases

BgeeiP29372.
CleanExiHS_MID1.
HS_MPG.
ExpressionAtlasiP29372. baseline and differential.
GenevestigatoriP29372.

Organism-specific databases

HPAiHPA006531.

Interactioni

Subunit structurei

Binds MBD1. Binds SSBP1.

Binary interactionsi

WithEntry#Exp.IntActNotes
PRNPP041564EBI-1043398,EBI-977302

Protein-protein interaction databases

BioGridi110490. 60 interactions.
IntActiP29372. 3 interactions.
MINTiMINT-135511.
STRINGi9606.ENSP00000219431.

Structurei

Secondary structure

1
298
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi82 – 843Combined sources
Helixi88 – 914Combined sources
Helixi95 – 1017Combined sources
Turni102 – 1043Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi116 – 12712Combined sources
Beta strandi129 – 1313Combined sources
Helixi138 – 1403Combined sources
Helixi145 – 1506Combined sources
Beta strandi155 – 1617Combined sources
Turni162 – 1643Combined sources
Beta strandi165 – 1717Combined sources
Beta strandi178 – 18811Combined sources
Helixi190 – 19910Combined sources
Helixi211 – 2133Combined sources
Beta strandi214 – 2174Combined sources
Helixi218 – 2247Combined sources
Helixi229 – 2313Combined sources
Turni236 – 2383Combined sources
Beta strandi240 – 2456Combined sources
Helixi253 – 2553Combined sources
Beta strandi256 – 2594Combined sources
Turni268 – 2725Combined sources
Beta strandi276 – 2794Combined sources
Turni290 – 2923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP29372. Positions 82-293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29372.

Family & Domainsi

Sequence similaritiesi

Belongs to the DNA glycosylase MPG family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2094.
GeneTreeiENSGT00390000009825.
HOGENOMiHOG000224224.
HOVERGENiHBG000019.
InParanoidiP29372.
KOiK03652.
OMAiTHYPLRF.
PhylomeDBiP29372.
TreeFamiTF331768.

Family and domain databases

Gene3Di3.10.300.10. 1 hit.
HAMAPiMF_00527. 3MGH.
InterProiIPR011034. Formyl_transferase_C-like.
IPR003180. PurDNA_glycsylse.
[Graphical view]
PANTHERiPTHR10429. PTHR10429. 1 hit.
PfamiPF02245. Pur_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
TIGRFAMsiTIGR00567. 3mg. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: P29372-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD
60 70 80 90 100
AAQAPCPRER CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR
110 120 130 140 150
AFLGQVLVRR LPNGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF
160 170 180 190 200
MKPGTLYVYI IYGMYFCMNI SSQGDGACVL LRALEPLEGL ETMRQLRSTL
210 220 230 240 250
RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE AVWLERGPLE
260 270 280 290
PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQA
Length:298
Mass (Da):32,869
Last modified:September 22, 2008 - v3
Checksum:iBEA8C4CB250D572B
GO
Isoform 2 (identifier: P29372-2) [UniParc]FASTAAdd to basket

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

Show »
Length:293
Mass (Da):32,181
Checksum:i81BE31859298D43C
GO
Isoform 3 (identifier: P29372-4) [UniParc]FASTAAdd to basket

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

Show »
Length:293
Mass (Da):32,186
Checksum:i6F710D76409B2D81
GO
Isoform 4 (identifier: P29372-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.

Note: Gene prediction based on EST data.

Show »
Length:281
Mass (Da):30,824
Checksum:i6826A6C692AABA9C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131Q → QV in AAK61213 (PubMed:11157797).Curated
Sequence conflicti29 – 313GQP → ARA in AAB19537 (PubMed:1874728).Curated
Sequence conflicti44 – 441Q → R in AAB19537 (PubMed:1874728).Curated
Sequence conflicti69 – 713GPY → SKD in AAA58369 (PubMed:1645538).Curated
Sequence conflicti69 – 713GPY → SKD in CAA39875 (PubMed:1645538).Curated
Sequence conflicti82 – 821H → L in AAA58369 (PubMed:1645538).Curated
Sequence conflicti82 – 821H → L in CAA39875 (PubMed:1645538).Curated
Sequence conflicti134 – 1341A → P in AAA58627 (PubMed:1924375).Curated
Sequence conflicti287 – 2871V → E in AAA58369 (PubMed:1645538).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221K → Q.1 Publication
Corresponds to variant rs3176383 [ dbSNP | Ensembl ].
VAR_019138
Natural varianti64 – 641P → L.
Corresponds to variant rs2308315 [ dbSNP | Ensembl ].
VAR_014831
Natural varianti71 – 711Y → H.1 Publication
Corresponds to variant rs2266607 [ dbSNP | Ensembl ].
VAR_014832
Natural varianti93 – 931Q → R.
Corresponds to variant rs25671 [ dbSNP | Ensembl ].
VAR_050096
Natural varianti120 – 1201R → C.
Corresponds to variant rs2308313 [ dbSNP | Ensembl ].
VAR_014833
Natural varianti141 – 1411R → Q.
Corresponds to variant rs2308312 [ dbSNP | Ensembl ].
VAR_014834
Natural varianti258 – 2581A → V.1 Publication
Corresponds to variant rs769193 [ dbSNP | Ensembl ].
VAR_014835
Natural varianti298 – 2981A → S.1 Publication
Corresponds to variant rs2234949 [ dbSNP | Ensembl ].
VAR_014836

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717Missing in isoform 4. CuratedVSP_046678Add
BLAST
Alternative sequencei1 – 1212MVTPA…MKKPK → MPARSGA in isoform 2 and isoform 3. 3 PublicationsVSP_003249Add
BLAST
Alternative sequencei195 – 1962QL → HV in isoform 2. 2 PublicationsVSP_035485

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32345.1. [P29372-4]
CCDS32346.1. [P29372-1]
CCDS42087.1. [P29372-5]
PIRiA40798.
A41230.
A47471.
JN0062.
RefSeqiNP_001015052.1. NM_001015052.2. [P29372-4]
NP_001015054.1. NM_001015054.2. [P29372-5]
NP_002425.2. NM_002434.3. [P29372-1]
UniGeneiHs.459596.

Genome annotation databases

EnsembliENST00000219431; ENSP00000219431; ENSG00000103152. [P29372-1]
ENST00000356432; ENSP00000348809; ENSG00000103152. [P29372-4]
ENST00000397817; ENSP00000380918; ENSG00000103152. [P29372-5]
GeneIDi4350.
KEGGihsa:4350.
UCSCiuc002cfm.4. human. [P29372-1]
uc002cfo.4. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32345.1. [P29372-4]
CCDS32346.1. [P29372-1]
CCDS42087.1. [P29372-5]
PIRiA40798.
A41230.
A47471.
JN0062.
RefSeqiNP_001015052.1. NM_001015052.2. [P29372-4]
NP_001015054.1. NM_001015054.2. [P29372-5]
NP_002425.2. NM_002434.3. [P29372-1]
UniGeneiHs.459596.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP29372. Positions 82-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110490. 60 interactions.
IntActiP29372. 3 interactions.
MINTiMINT-135511.
STRINGi9606.ENSP00000219431.

PTM databases

PhosphoSiteiP29372.

Proteomic databases

MaxQBiP29372.
PaxDbiP29372.
PRIDEiP29372.

Protocols and materials databases

DNASUi4350.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219431; ENSP00000219431; ENSG00000103152. [P29372-1]
ENST00000356432; ENSP00000348809; ENSG00000103152. [P29372-4]
ENST00000397817; ENSP00000380918; ENSG00000103152. [P29372-5]
GeneIDi4350.
KEGGihsa:4350.
UCSCiuc002cfm.4. human. [P29372-1]
uc002cfo.4. human.

Organism-specific databases

CTDi4350.
GeneCardsiGC16P000127.
HGNCiHGNC:7211. MPG.
HPAiHPA006531.
MIMi156565. gene.
neXtProtiNX_P29372.
PharmGKBiPA30917.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2094.
GeneTreeiENSGT00390000009825.
HOGENOMiHOG000224224.
HOVERGENiHBG000019.
InParanoidiP29372.
KOiK03652.
OMAiTHYPLRF.
PhylomeDBiP29372.
TreeFamiTF331768.

Enzyme and pathway databases

BRENDAi3.2.2.21. 2681.
ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
REACT_1729. Cleavage of the damaged purine.
REACT_2176. Recognition and association of DNA glycosylase with site containing an affected purine.

Miscellaneous databases

ChiTaRSiMPG. human.
EvolutionaryTraceiP29372.
GeneWikiiMPG_(gene).
GenomeRNAii4350.
NextBioi17110.
PROiP29372.
SOURCEiSearch...

Gene expression databases

BgeeiP29372.
CleanExiHS_MID1.
HS_MPG.
ExpressionAtlasiP29372. baseline and differential.
GenevestigatoriP29372.

Family and domain databases

Gene3Di3.10.300.10. 1 hit.
HAMAPiMF_00527. 3MGH.
InterProiIPR011034. Formyl_transferase_C-like.
IPR003180. PurDNA_glycsylse.
[Graphical view]
PANTHERiPTHR10429. PTHR10429. 1 hit.
PfamiPF02245. Pur_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
TIGRFAMsiTIGR00567. 3mg. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1990) [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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Identification of a human cell proliferation gene 11."
    Kim J.W.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. NIEHS SNPs program
    Submitted (MAR-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(2000) [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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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(2003) [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(1990) [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(1990) [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(1992) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBD1.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and interacts with mitochondrial single-stranded binding protein (mtSSB)."
    van Loon B., Samson L.D.
    DNA Repair 12:177-187(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SSBP1, ENZYME REGULATION.
  16. "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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 80-199.

Entry informationi

Entry namei3MG_HUMAN
AccessioniPrimary (citable) accession number: P29372
Secondary accession number(s): G5E9E2
, Q13770, Q15275, Q15961, Q5J9I4, Q96BZ6, Q96S33, Q9NNX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 1992
Last sequence update: September 22, 2008
Last modified: March 31, 2015
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.