HUMAN:TDG

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TDG
Protein Name(s)	G/T mismatch-specific thymine DNA glycosylase Thymine-DNA glycosylase hTDG
External Links
UniProt	Q13569
EMBL	U51166 AF545435 AC078819 BC037557
CCDS	CCDS9095.1
RefSeq	NP_003202.3
UniGene	Hs.584809
PDB	1WYW 2D07 2RBA 3UFJ 3UO7 3UOB 4FNC 4JGC
PDBsum	1WYW 2D07 2RBA 3UFJ 3UO7 3UOB 4FNC 4JGC
DisProt	DP00719
ProteinModelPortal	Q13569
SMR	Q13569
BioGrid	112855
DIP	DIP-32709N
IntAct	Q13569
MINT	MINT-1182514
STRING	9606.ENSP00000376611
PhosphoSite	Q13569
DMDM	46397791
MaxQB	Q13569
PaxDb	Q13569
PRIDE	Q13569
Ensembl	ENST00000392872
GeneID	6996
KEGG	hsa:6996
UCSC	uc001tkg.3
CTD	6996
GeneCards	GC12P104359
H-InvDB	HIX0026376
HGNC	HGNC:11700
HPA	HPA052263
MIM	601423
neXtProt	NX_Q13569
PharmGKB	PA36419
eggNOG	COG3663
GeneTree	ENSGT00390000000987
HOGENOM	HOG000220820
HOVERGEN	HBG003685
InParanoid	Q13569
KO	K03649
OMA	NGQWMTQ
OrthoDB	EOG790G1Z
PhylomeDB	Q13569
TreeFam	TF328764
Reactome	REACT_1064 REACT_200682 REACT_702
ChiTaRS	TDG
EvolutionaryTrace	Q13569
GeneWiki	Thymine-DNA_glycosylase
GenomeRNAi	6996
NextBio	27327
PRO	PR:Q13569
Proteomes	UP000005640
Bgee	Q13569
CleanEx	HS_TDG
ExpressionAtlas	Q13569
Genevestigator	Q13569
GO	GO:0005654 GO:0005634 GO:0005886 GO:0016605 GO:0003684 GO:0019104 GO:0003690 GO:0030983 GO:0042803 GO:0008263 GO:0001104 GO:0043566 GO:0006284 GO:0006285 GO:0016568 GO:0045008 GO:0080111 GO:0006281 GO:0009790 GO:0006298 GO:0035562 GO:0032091 GO:0000122 GO:0040029
Gene3D	3.40.470.10
InterPro	IPR015637 IPR003310 IPR005122
PANTHER	PTHR12159
Pfam	PF03167
SMART	SM00986
SUPFAM	SSF52141
TIGRFAMs	TIGR00584

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0006284	base-excision repair	PMID:24948610^[1]	ECO:0000314			P	Figure 4	complete CACAO 10659
enables	GO:0031402	sodium ion binding	PMID:15959518^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:15959518^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0031404	chloride ion binding	PMID:15959518^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0030983	mismatched DNA binding	PMID:15959518^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008263	pyrimidine-specific mismatch base pair DNA N-glycosylase activity	PMID:11889051^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	PMID:11889051^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004844	uracil DNA N-glycosylase activity	PMID:11889051^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006285	base-excision repair, AP site formation	PMID:11889051^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0032183	SUMO binding	PMID:15959518^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P63165	F	Seeded From UniProt	complete
enables	GO:0030983	mismatched DNA binding	PMID:16626738^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0032183	SUMO binding	PMID:16626738^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55854	F	Seeded From UniProt	complete
enables	GO:0032183	SUMO binding	PMID:11889051^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55854	F	Seeded From UniProt	complete
enables	GO:0032183	SUMO binding	PMID:11889051^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P63165	F	Seeded From UniProt	complete
involved_in	GO:1902544	regulation of DNA N-glycosylase activity	PMID:18512959^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006285	base-excision repair, AP site formation	PMID:18512959^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008263	pyrimidine-specific mismatch base pair DNA N-glycosylase activity	PMID:18512959^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043739	G/U mismatch-specific uracil-DNA glycosylase activity	PMID:18512959^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043621	protein self-association	PMID:18512959^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0030983	mismatched DNA binding	PMID:18512959^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	PMID:18512959^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:11889051^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11889051^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0030983	mismatched DNA binding	PMID:11889051^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0080111	DNA demethylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P56581	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P56581	F	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:22327402^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0040029	regulation of gene expression, epigenetic	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P56581	P	Seeded From UniProt	complete
enables	GO:0030983	mismatched DNA binding	PMID:22573813^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	PMID:21862836^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	PMID:22327402^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0045995	regulation of embryonic development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P56581	P	Seeded From UniProt	complete
enables	GO:0008263	pyrimidine-specific mismatch base pair DNA N-glycosylase activity	PMID:8662714^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008263	pyrimidine-specific mismatch base pair DNA N-glycosylase activity	PMID:22573813^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006298	mismatch repair	PMID:22573813^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:21862836^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:22327402^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:8662714^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	PMID:22327402^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008263	pyrimidine-specific mismatch base pair DNA N-glycosylase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0026869 PANTHER:PTN000255408 UniProtKB:Q13569	F	Seeded From UniProt	complete
involved_in	GO:0006285	base-excision repair, AP site formation	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000255408 UniProtKB:Q13569	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:108247 PANTHER:PTN000952417 RGD:620959 UniProtKB:Q13569	C	Seeded From UniProt	complete
enables	GO:0004844	uracil DNA N-glycosylase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000255408 PomBase:SPCC965.05c UniProtKB:Q13569	F	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0080111	DNA demethylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	P	Seeded From UniProt	complete
involved_in	GO:0045995	regulation of embryonic development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	P	Seeded From UniProt	complete
involved_in	GO:0040029	regulation of gene expression, epigenetic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	P	Seeded From UniProt	complete
involved_in	GO:0035562	negative regulation of chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	P	Seeded From UniProt	complete
enables	GO:0032183	SUMO binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	F	Seeded From UniProt	complete
involved_in	GO:0032091	negative regulation of protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	P	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	F	Seeded From UniProt	complete
part_of	GO:0016605	PML body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	C	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	C	Seeded From UniProt	complete
enables	GO:0005080	protein kinase C binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	F	Seeded From UniProt	complete
enables	GO:0003712	transcription coregulator activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	F	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P56581 ensembl:ENSMUSP00000121000	P	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A096MIY3 ensembl:ENSRNOP00000067921	F	Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A096MIY3 ensembl:ENSRNOP00000067921	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A096MIY3 ensembl:ENSRNOP00000067921	C	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A096MIY3 ensembl:ENSRNOP00000067921	P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003310 InterPro:IPR015637	P	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003310 InterPro:IPR015637	F	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:9489705^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:9489705^[11] Reactome:R-HSA-5221061 Reactome:R-HSA-5220959 Reactome:R-HSA-4551738 Reactome:R-HSA-4551648 Reactome:R-HSA-110350 Reactome:R-HSA-110234 Reactome:R-HSA-110219 Reactome:R-HSA-110218 Reactome:R-HSA-110210 Reactome:R-HSA-110159 Reactome:R-HSA-110158	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:9489705^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0045008	depyrimidination	Reactome:R-HSA-110329 Reactome:R-HSA-110328	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0035511	oxidative DNA demethylation	Reactome:R-HSA-5221061 Reactome:R-HSA-5220959	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	Reactome:R-HSA-5221061 Reactome:R-HSA-5220959 Reactome:R-HSA-110234 Reactome:R-HSA-110219 Reactome:R-HSA-110218	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
involved_in	GO:0006325	chromatin organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0156	P	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Müller, U et al. (2014) TET-mediated oxidation of methylcytosine causes TDG or NEIL glycosylase dependent gene reactivation. Nucleic Acids Res. 42 8592-604 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Baba, D et al. (2005) Crystal structure of thymine DNA glycosylase conjugated to SUMO-1. Nature 435 979-82 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 ^3.8 Hardeland, U et al. (2002) Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 21 1456-64 PubMed GONUTS page
↑ ^4.0 ^4.1 Baba, D et al. (2006) Crystal structure of SUMO-3-modified thymine-DNA glycosylase. J. Mol. Biol. 359 137-47 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Smet-Nocca, C et al. (2008) The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. Biochemistry 47 6519-30 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Zhang, L et al. (2012) Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA. Nat. Chem. Biol. 8 328-30 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Maiti, A et al. (2012) Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA. Proc. Natl. Acad. Sci. U.S.A. 109 8091-6 PubMed GONUTS page
↑ ^8.0 ^8.1 Maiti, A & Drohat, AC (2011) Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites. J. Biol. Chem. 286 35334-8 PubMed GONUTS page
↑ ^9.0 ^9.1 Neddermann, P et al. (1996) Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase. J. Biol. Chem. 271 12767-74 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Barrett, TE et al. (1998) Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92 117-29 PubMed GONUTS page

[PMID:24948610-1] Müller, U et al. (2014) TET-mediated oxidation of methylcytosine causes TDG or NEIL glycosylase dependent gene reactivation. Nucleic Acids Res. 42 8592-604 PubMed GONUTS page

[PMID:15959518-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Baba, D et al. (2005) Crystal structure of thymine DNA glycosylase conjugated to SUMO-1. Nature 435 979-82 PubMed GONUTS page

[PMID:11889051-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 ^3.8 Hardeland, U et al. (2002) Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 21 1456-64 PubMed GONUTS page

[PMID:16626738-4] 4.0 ^4.1 Baba, D et al. (2006) Crystal structure of SUMO-3-modified thymine-DNA glycosylase. J. Mol. Biol. 359 137-47 PubMed GONUTS page

[PMID:18512959-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Smet-Nocca, C et al. (2008) The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. Biochemistry 47 6519-30 PubMed GONUTS page

[PMID:22327402-6] 6.0 ^6.1 ^6.2 ^6.3 Zhang, L et al. (2012) Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA. Nat. Chem. Biol. 8 328-30 PubMed GONUTS page

[PMID:22573813-7] 7.0 ^7.1 ^7.2 Maiti, A et al. (2012) Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA. Proc. Natl. Acad. Sci. U.S.A. 109 8091-6 PubMed GONUTS page

[PMID:21862836-8] 8.0 ^8.1 Maiti, A & Drohat, AC (2011) Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites. J. Biol. Chem. 286 35334-8 PubMed GONUTS page

[PMID:8662714-9] 9.0 ^9.1 Neddermann, P et al. (1996) Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase. J. Biol. Chem. 271 12767-74 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 ^10.2 ^10.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:9489705-11] 11.0 ^11.1 ^11.2 Barrett, TE et al. (1998) Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92 117-29 PubMed GONUTS page

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HUMAN:TDG

Contents

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References

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