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P29372

- 3MG_HUMAN

UniProt

P29372 - 3MG_HUMAN

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Protein

DNA-3-methyladenine glycosylase

Gene
MPG, AAG, ANPG, MID1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

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
Complete GO annotation...

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. Mitochondrion matrixmitochondrion nucleoid. 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 – 1717Mitochondrion Reviewed predictionAdd
BLAST
Chaini18 – 298281DNA-3-methyladenine glycosylaseUniRule annotationPRO_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.

Miscellaneous databases

EvolutionaryTraceiP29372.

Family & Domainsi

Sequence similaritiesi

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

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. VSP_046678Add
BLAST
Alternative sequencei1 – 1212MVTPA…MKKPK → MPARSGA in isoform 2 and isoform 3. VSP_003249Add
BLAST
Alternative sequencei195 – 1962QL → HV in isoform 2. VSP_035485

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131Q → QV in AAK61213. 1 Publication
Sequence conflicti29 – 313GQP → ARA in AAB19537. 1 Publication
Sequence conflicti44 – 441Q → R in AAB19537. 1 Publication
Sequence conflicti69 – 713GPY → SKD in AAA58369. 1 Publication
Sequence conflicti69 – 713GPY → SKD in CAA39875. 1 Publication
Sequence conflicti82 – 821H → L in AAA58369. 1 Publication
Sequence conflicti82 – 821H → L in CAA39875. 1 Publication
Sequence conflicti134 – 1341A → P in AAA58627. 1 Publication
Sequence conflicti287 – 2871V → E in AAA58369. 1 Publication

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

« 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(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: September 3, 2014
This is version 160 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

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