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P29372

- 3MG_HUMAN

UniProt

P29372 - 3MG_HUMAN

Protein

DNA-3-methyladenine glycosylase

Gene

MPG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (23 Sep 2008)
      Previous versions | rss
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    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: RefGenome
    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
    7. protein binding Source: IntAct

    GO - Biological processi

    1. base-excision repair Source: RefGenome
    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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

    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: 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

    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

    ArrayExpressiP29372.
    BgeeiP29372.
    CleanExiHS_MID1.
    HS_MPG.
    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. 56 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 – 843
    Helixi88 – 914
    Helixi95 – 1017
    Turni102 – 1043
    Beta strandi106 – 1105
    Beta strandi116 – 12712
    Beta strandi129 – 1313
    Helixi138 – 1403
    Helixi145 – 1506
    Beta strandi155 – 1617
    Turni162 – 1643
    Beta strandi165 – 1717
    Beta strandi178 – 18811
    Helixi190 – 19910
    Helixi211 – 2133
    Beta strandi214 – 2174
    Helixi218 – 2247
    Helixi229 – 2313
    Turni236 – 2383
    Beta strandi240 – 2456
    Helixi253 – 2553
    Beta strandi256 – 2594
    Turni268 – 2725
    Beta strandi276 – 2794
    Turni290 – 2923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliP29372.
    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.
    HOGENOMiHOG000224224.
    HOVERGENiHBG000019.
    InParanoidiP29372.
    KOiK03652.
    OMAiTIYVYPI.
    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. Align

    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

    MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD    50
    AAQAPCPRER CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR 100
    AFLGQVLVRR LPNGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF 150
    MKPGTLYVYI IYGMYFCMNI SSQGDGACVL LRALEPLEGL ETMRQLRSTL 200
    RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE AVWLERGPLE 250
    PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQA 298
    Length:298
    Mass (Da):32,869
    Last modified:September 23, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS32345.1. [P29372-4 ]
    CCDS32346.1. [P29372-1 ]
    CCDS42087.1. [P29372-5 ]
    PIRi A40798.
    A41230.
    A47471.
    JN0062.
    RefSeqi NP_001015052.1. NM_001015052.2. [P29372-4 ]
    NP_001015054.1. NM_001015054.2. [P29372-5 ]
    NP_002425.2. NM_002434.3. [P29372-1 ]
    UniGenei Hs.459596.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    3QI5 X-ray 2.20 A/B 84-298 [» ]
    3UBY X-ray 2.00 A/B 84-298 [» ]
    ProteinModelPortali P29372.
    SMRi P29372. Positions 82-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110490. 56 interactions.
    IntActi P29372. 3 interactions.
    MINTi MINT-135511.
    STRINGi 9606.ENSP00000219431.

    PTM databases

    PhosphoSitei P29372.

    Proteomic databases

    MaxQBi P29372.
    PaxDbi P29372.
    PRIDEi P29372.

    Protocols and materials databases

    DNASUi 4350.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219431 ; ENSP00000219431 ; ENSG00000103152 . [P29372-1 ]
    ENST00000356432 ; ENSP00000348809 ; ENSG00000103152 . [P29372-4 ]
    ENST00000397817 ; ENSP00000380918 ; ENSG00000103152 . [P29372-5 ]
    GeneIDi 4350.
    KEGGi hsa:4350.
    UCSCi uc002cfm.4. human. [P29372-1 ]
    uc002cfo.4. human.

    Organism-specific databases

    CTDi 4350.
    GeneCardsi GC16P000127.
    HGNCi HGNC:7211. MPG.
    HPAi HPA006531.
    MIMi 156565. gene.
    neXtProti NX_P29372.
    PharmGKBi PA30917.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2094.
    HOGENOMi HOG000224224.
    HOVERGENi HBG000019.
    InParanoidi P29372.
    KOi K03652.
    OMAi TIYVYPI.
    PhylomeDBi P29372.
    TreeFami TF331768.

    Enzyme and pathway databases

    Reactomei REACT_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

    ChiTaRSi MPG. human.
    EvolutionaryTracei P29372.
    GeneWikii MPG_(gene).
    GenomeRNAii 4350.
    NextBioi 17110.
    PROi P29372.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29372.
    Bgeei P29372.
    CleanExi HS_MID1.
    HS_MPG.
    Genevestigatori P29372.

    Family and domain databases

    Gene3Di 3.10.300.10. 1 hit.
    HAMAPi MF_00527. 3MGH.
    InterProi IPR011034. Formyl_transferase_C-like.
    IPR003180. PurDNA_glycsylse.
    [Graphical view ]
    PANTHERi PTHR10429. PTHR10429. 1 hit.
    Pfami PF02245. Pur_DNA_glyco. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50486. SSF50486. 1 hit.
    TIGRFAMsi TIGR00567. 3mg. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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(2013) [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(1998) [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: December 1, 1992
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 161 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