GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Endonuclease III-like protein 1 (hNTH1) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)

 NTH_HUMAN               Reviewed;         312 AA.
P78549; Q1MVR1; Q99566; Q99794; Q9BPX2;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 2.
31-JUL-2019, entry version 184.
RecName: Full=Endonuclease III-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03183};
Short=hNTH1;
EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03183};
EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_03183};
AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_03183};
Short=DNA glycosylase/AP lyase {ECO:0000255|HAMAP-Rule:MF_03183};
Flags: Precursor;
Name=NTHL1 {ECO:0000255|HAMAP-Rule:MF_03183}; Synonyms=NTH1, OCTS3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAM11786.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=8990169; DOI=10.1073/pnas.94.1.109;
Aspinwall R., Rothwell D.G., Roldan-Arjona T., Anselmino C.,
Ward C.J., Cheadle J.P., Sampson J.R., Lindahl T., Harris P.C.,
Hickson I.D.;
"Cloning and characterization of a functional human homolog of
Escherichia coli endonuclease III.";
Proc. Natl. Acad. Sci. U.S.A. 94:109-114(1997).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND TISSUE
SPECIFICITY.
TISSUE=Placenta;
PubMed=9831664; DOI=10.1016/S0378-1119(98)00485-5;
Imai K., Sarker A.H., Akiyama K., Ikeda S., Yao M., Tsutsui K.,
Shohmori T., Seki S.;
"Genomic structure and sequence of a human homologue (NTHL1/NTH1) of
Escherichia coli endonuclease III with those of the adjacent parts of
TSC2 and SLC9A3R2 genes.";
Gene 222:287-295(1998).
[3] {ECO:0000305, ECO:0000312|EMBL:AAM11786.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-21 AND LEU-234.
NIEHS SNPs program;
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
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.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ACTIVE SITE, AND
MUTAGENESIS OF LYS-220.
TISSUE=Bone marrow;
PubMed=9705289; DOI=10.1074/jbc.273.34.21585;
Ikeda S., Biswas T., Roy R., Izumi T., Boldogh I., Kurosky A.,
Sarker A.H., Seki S., Mitra S.;
"Purification and characterization of human NTH1, a homolog of
Escherichia coli endonuclease III. Direct identification of Lys-212 as
the active nucleophilic residue.";
J. Biol. Chem. 273:21585-21593(1998).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
TISSUE=Spleen;
PubMed=9045706; DOI=10.1074/jbc.272.10.6733;
Hilbert T.P., Chaung W., Boorstein R.J., Cunningham R.P., Teebor G.W.;
"Cloning and expression of the cDNA encoding the human homologue of
the DNA repair enzyme, Escherichia coli endonuclease III.";
J. Biol. Chem. 272:6733-6740(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-312 (ISOFORMS 1 AND 2).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 9-312, FUNCTION, SUBCELLULAR LOCATION,
AND DEVELOPMENTAL STAGE.
PubMed=10882850; DOI=10.1016/S0921-8777(00)00015-X;
Luna L., Bjoras M., Hoff E., Rognes T., Seeberg E.;
"Cell-cycle regulation, intracellular sorting and induced
overexpression of the human NTH1 DNA glycosylase involved in removal
of formamidopyrimidine residues from DNA.";
Mutat. Res. 460:95-104(2000).
[9]
PROTEIN SEQUENCE OF 31-37; 48-56; 61-78; 107-113; 120-126 AND 221-227,
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=12144783; DOI=10.1016/S0022-2836(02)00623-X;
Liu X., Roy R.;
"Truncation of amino-terminal tail stimulates activity of human
endonuclease III (hNTH1).";
J. Mol. Biol. 321:265-276(2002).
[10]
SUBCELLULAR LOCATION.
PubMed=9611236; DOI=10.1093/nar/26.12.2917;
Takao M., Aburatani H., Kobayashi K., Yasui A.;
"Mitochondrial targeting of human DNA glycosylases for repair of
oxidative DNA damage.";
Nucleic Acids Res. 26:2917-2922(1998).
[11]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9890904; DOI=10.1021/bi9819071;
Dizdaroglu M., Karahalil B., Senturker S., Buckley T.J.,
Roldan-Arjona T.;
"Excision of products of oxidative DNA base damage by human NTH1
protein.";
Biochemistry 38:243-246(1999).
[12]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11380260; DOI=10.1021/bi0028901;
Eide L., Luna L., Gustad E.C., Henderson P.T., Essigmann J.M.,
Demple B., Seeberg E.;
"Human endonuclease III acts preferentially on DNA damage opposite
guanine residues in DNA.";
Biochemistry 40:6653-6659(2001).
[13]
FUNCTION, AND MUTAGENESIS OF LYS-220.
PubMed=11695910; DOI=10.1021/bi011053b;
Liu X., Roy R.;
"Mutation at active site lysine 212 to arginine uncouples the
glycosylase activity from the lyase activity of human endonuclease
III.";
Biochemistry 40:13617-13622(2001).
[14]
CATALYTIC ACTIVITY, INTERACTION WITH YBX1, AND ACTIVITY REGULATION.
PubMed=11287425; DOI=10.1074/jbc.M101594200;
Marenstein D.R., Ocampo M.T., Chan M.K., Altamirano A., Basu A.K.,
Boorstein R.J., Cunningham R.P., Teebor G.W.;
"Stimulation of human endonuclease III by Y box-binding protein 1
(DNA-binding protein B). Interaction between a base excision repair
enzyme and a transcription factor.";
J. Biol. Chem. 276:21242-21249(2001).
[15]
FUNCTION.
PubMed=11328882; DOI=10.1093/nar/29.9.1975;
Matsumoto Y., Zhang Q.M., Takao M., Yasui A., Yonei S.;
"Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in
removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA.";
Nucleic Acids Res. 29:1975-1981(2001).
[16] {ECO:0000305}
SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, AND MUTAGENESIS OF
40-ARG--ARG-42; ARG-42 AND ARG-57.
PubMed=12531031; DOI=10.1016/S1568-7864(02)00145-3;
Ikeda S., Kohmoto T., Tabata R., Seki Y.;
"Differential intracellular localization of the human and mouse
endonuclease III homologs and analysis of the sorting signals.";
DNA Repair 1:847-854(2002).
[17]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=12140329; DOI=10.1093/nar/gkf460;
Miyabe I., Zhang Q.M., Kino K., Sugiyama H., Takao M., Yasui A.,
Yonei S.;
"Identification of 5-formyluracil DNA glycosylase activity of human
hNTH1 protein.";
Nucleic Acids Res. 30:3443-3448(2002).
[18]
FUNCTION, SUBSTRATES, AND ACTIVITY REGULATION.
PubMed=12519758; DOI=10.1074/jbc.M212168200;
Marenstein D.R., Chan M.K., Altamirano A., Basu A.K., Boorstein R.J.,
Cunningham R.P., Teebor G.W.;
"Substrate specificity of human endonuclease III (hNTH1). Effect of
human APE1 on hNTH1 activity.";
J. Biol. Chem. 278:9005-9012(2003).
[19]
FUNCTION, AND SUBSTRATES.
PubMed=14734554; DOI=10.1074/jbc.M400393200;
Katafuchi A., Nakano T., Masaoka A., Terato H., Iwai S., Hanaoka F.,
Ide H.;
"Differential specificity of human and Escherichia coli endonuclease
III and VIII homologues for oxidative base lesions.";
J. Biol. Chem. 279:14464-14471(2004).
[20]
FUNCTION, AND SUBSTRATES.
PubMed=15533839; DOI=10.1016/j.dnarep.2004.08.002;
Zhang Q.M., Yonekura S., Takao M., Yasui A., Sugiyama H., Yonei S.;
"DNA glycosylase activities for thymine residues oxidized in the
methyl group are functions of the hNEIL1 and hNTH1 enzymes in human
cells.";
DNA Repair 4:71-79(2005).
[21]
FUNCTION.
PubMed=17923696; DOI=10.1128/MCB.00791-07;
Prasad A., Wallace S.S., Pederson D.S.;
"Initiation of base excision repair of oxidative lesions in
nucleosomes by the human, bifunctional DNA glycosylase NTH1.";
Mol. Cell. Biol. 27:8442-8453(2007).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
FUNCTION.
PubMed=20005182; DOI=10.1016/j.dnarep.2009.11.005;
Odell I.D., Newick K., Heintz N.H., Wallace S.S., Pederson D.S.;
"Non-specific DNA binding interferes with the efficient excision of
oxidative lesions from chromatin by the human DNA glycosylase,
NEIL1.";
DNA Repair 9:134-143(2010).
[24]
FUNCTION.
PubMed=20110254; DOI=10.1093/nar/gkq022;
Matsumoto N., Toga T., Hayashi R., Sugasawa K., Katayanagi K., Ide H.,
Kuraoka I., Iwai S.;
"Fluorescent probes for the analysis of DNA strand scission in base
excision repair.";
Nucleic Acids Res. 38:E101-E101(2010).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
FUNCTION.
PubMed=21930793; DOI=10.1128/MCB.05715-11;
Odell I.D., Barbour J.E., Murphy D.L., Della-Maria J.A., Sweasy J.B.,
Tomkinson A.E., Wallace S.S., Pederson D.S.;
"Nucleosome disruption by DNA ligase III-XRCC1 promotes efficient base
excision repair.";
Mol. Cell. Biol. 31:4623-4632(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-73, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
INVOLVEMENT IN FAP3.
PubMed=25938944; DOI=10.1038/ng.3287;
Weren R.D., Ligtenberg M.J., Kets C.M., de Voer R.M., Verwiel E.T.,
Spruijt L., van Zelst-Stams W.A., Jongmans M.C., Gilissen C.,
Hehir-Kwa J.Y., Hoischen A., Shendure J., Boyle E.A., Kamping E.J.,
Nagtegaal I.D., Tops B.B., Nagengast F.M., Geurts van Kessel A.,
van Krieken J.H., Kuiper R.P., Hoogerbrugge N.;
"A germline homozygous mutation in the base-excision repair gene NTHL1
causes adenomatous polyposis and colorectal cancer.";
Nat. Genet. 47:668-671(2015).
-!- FUNCTION: Bifunctional DNA N-glycosylase with associated
apurinic/apyrimidinic (AP) lyase function that catalyzes the first
step in base excision repair (BER), the primary repair pathway for
the repair of oxidative DNA damage. The DNA N-glycosylase activity
releases the damaged DNA base from DNA by cleaving the N-
glycosidic bond, leaving an AP site. The AP-lyase activity cleaves
the phosphodiester bond 3' to the AP site by a beta-elimination.
Primarily recognizes and repairs oxidative base damage of
pyrimidines. Has also 8-oxo-7,8-dihydroguanine (8-oxoG) DNA
glycosylase activity. Acts preferentially on DNA damage opposite
guanine residues in DNA. Is able to process lesions in nucleosomes
without requiring or inducing nucleosome disruption.
{ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:10882850,
ECO:0000269|PubMed:11328882, ECO:0000269|PubMed:11380260,
ECO:0000269|PubMed:11695910, ECO:0000269|PubMed:12140329,
ECO:0000269|PubMed:12144783, ECO:0000269|PubMed:12519758,
ECO:0000269|PubMed:14734554, ECO:0000269|PubMed:15533839,
ECO:0000269|PubMed:17923696, ECO:0000269|PubMed:20005182,
ECO:0000269|PubMed:20110254, ECO:0000269|PubMed:21930793,
ECO:0000269|PubMed:8990169, ECO:0000269|PubMed:9045706,
ECO:0000269|PubMed:9705289, ECO:0000269|PubMed:9890904}.
-!- CATALYTIC ACTIVITY:
Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in
DNA is broken by a beta-elimination reaction, leaving a 3'-
terminal unsaturated sugar and a product with a terminal 5'-
phosphate.; EC=4.2.99.18;
Evidence={ECO:0000250|UniProtKB:P20625, ECO:0000255|HAMAP-
Rule:MF_03183, ECO:0000269|PubMed:11287425,
ECO:0000269|PubMed:12140329, ECO:0000269|PubMed:12144783};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000255|HAMAP-Rule:MF_03183};
Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play
a role in catalysis, but is probably involved in the proper
positioning of the enzyme along the DNA strand.
{ECO:0000255|HAMAP-Rule:MF_03183};
-!- ACTIVITY REGULATION: APE1 displaces NTHL1 from the N-glycosylase-
generated AP site in DNA, thereby increasing the turnover of the
DNA N-glycosylase activity. AP lyase activity is stimulated by
YBX1. {ECO:0000269|PubMed:11287425, ECO:0000269|PubMed:12519758}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=371 nM for 5-hydroxy-6-hydrothymine containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:11380260, ECO:0000269|PubMed:9890904};
KM=1093 nM for 5-hydroxyuracil containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:11380260, ECO:0000269|PubMed:9890904};
KM=548 nM for 5-hydroxycytosine containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:11380260, ECO:0000269|PubMed:9890904};
KM=1101 nM for thymine glycol containing duplex oligonucleotides
(N-glycosylase activity) {ECO:0000269|PubMed:11380260,
ECO:0000269|PubMed:9890904};
KM=718 nM for 5,6-dihydroxycytosine containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:11380260, ECO:0000269|PubMed:9890904};
KM=0.05 nM for 5-hydroxycytosine-G containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:11380260, ECO:0000269|PubMed:9890904};
KM=0.2 nM for 5-hydroxycytosine-A containing duplex
oligonucleotides (N-glycosylase activity)
{ECO:0000269|PubMed:11380260, ECO:0000269|PubMed:9890904};
-!- SUBUNIT: Interacts with YBX1. {ECO:0000255|HAMAP-Rule:MF_03183,
ECO:0000269|PubMed:11287425}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183,
ECO:0000269|PubMed:10882850, ECO:0000269|PubMed:12531031,
ECO:0000269|PubMed:9611236}. Mitochondrion {ECO:0000255|HAMAP-
Rule:MF_03183, ECO:0000269|PubMed:9611236}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=1; Synonyms=M-8;
IsoId=P78549-1; Sequence=Displayed;
Name=2; Synonyms=M+1;
IsoId=P78549-2; Sequence=VSP_054293;
Name=3; Synonyms=M+8;
IsoId=P78549-3; Sequence=VSP_054292;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart
and lowest levels in lung and liver. {ECO:0000269|PubMed:8990169,
ECO:0000269|PubMed:9831664}.
-!- DEVELOPMENTAL STAGE: Expression levels are regulated during the
cell cycle with increased levels during early and mid S-phase.
{ECO:0000269|PubMed:10882850}.
-!- DISEASE: Familial adenomatous polyposis 3 (FAP3) [MIM:616415]: A
form of familial adenomatous polyposis, a condition characterized
by the development of multiple colorectal adenomatous polyps,
benign neoplasms derived from glandular epithelium. Some affected
individuals may develop colorectal carcinoma.
{ECO:0000269|PubMed:25938944}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP-
Rule:MF_03183}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/nthl1/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U79718; AAB41534.1; -; mRNA.
EMBL; AB014460; BAA32695.1; -; Genomic_DNA.
EMBL; AF498098; AAM11786.1; -; Genomic_DNA.
EMBL; AC005600; AAC34209.1; -; Genomic_DNA.
EMBL; AB001575; BAA19413.1; -; mRNA.
EMBL; U81285; AAC51136.1; -; mRNA.
EMBL; BC003014; AAH03014.1; -; mRNA.
EMBL; BC000391; AAH00391.2; -; mRNA.
EMBL; Y09687; CAA70865.1; -; mRNA.
CCDS; CCDS10457.1; -. [P78549-2]
RefSeq; NP_001305122.1; NM_001318193.1.
RefSeq; NP_001305123.1; NM_001318194.1.
RefSeq; NP_002519.1; NM_002528.6. [P78549-2]
SMR; P78549; -.
BioGrid; 110968; 25.
IntAct; P78549; 4.
STRING; 9606.ENSP00000219066; -.
iPTMnet; P78549; -.
PhosphoSitePlus; P78549; -.
BioMuta; NTHL1; -.
DMDM; 29840795; -.
EPD; P78549; -.
jPOST; P78549; -.
MaxQB; P78549; -.
PaxDb; P78549; -.
PeptideAtlas; P78549; -.
PRIDE; P78549; -.
ProteomicsDB; 57648; -. [P78549-1]
GeneID; 4913; -.
KEGG; hsa:4913; -.
UCSC; uc002col.1; human. [P78549-1]
CTD; 4913; -.
DisGeNET; 4913; -.
GeneCards; NTHL1; -.
HGNC; HGNC:8028; NTHL1.
HPA; CAB025152; -.
MalaCards; NTHL1; -.
MIM; 602656; gene.
MIM; 616415; phenotype.
neXtProt; NX_P78549; -.
OpenTargets; ENSG00000065057; -.
Orphanet; 454840; NTHL1-related attenuated familial adenomatous polyposis.
PharmGKB; PA31811; -.
eggNOG; KOG1921; Eukaryota.
eggNOG; COG0177; LUCA.
GeneTree; ENSGT00510000047513; -.
HOGENOM; HOG000252209; -.
InParanoid; P78549; -.
KO; K10773; -.
OMA; WQQFTHL; -.
OrthoDB; 1322642at2759; -.
PhylomeDB; P78549; -.
TreeFam; TF314967; -.
BRENDA; 4.2.99.18; 2681.
Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
Reactome; R-HSA-9630221; Defective NTHL1 substrate processing.
Reactome; R-HSA-9630222; Defective NTHL1 substrate binding.
SABIO-RK; P78549; -.
GeneWiki; NTHL1; -.
GenomeRNAi; 4913; -.
PRO; PR:P78549; -.
Proteomes; UP000005640; Unplaced.
Bgee; ENSG00000065057; Expressed in 173 organ(s), highest expression level in right lobe of liver.
ExpressionAtlas; P78549; baseline and differential.
Genevisible; P78549; HS.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:FlyBase.
GO; GO:0019104; F:DNA N-glycosylase activity; IDA:UniProtKB.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0004519; F:endonuclease activity; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; TAS:Reactome.
GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central.
GO; GO:0006285; P:base-excision repair, AP site formation; IDA:UniProtKB.
GO; GO:0045008; P:depyrimidination; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IDA:UniProtKB.
CDD; cd00056; ENDO3c; 1.
Gene3D; 1.10.1670.10; -; 1.
HAMAP; MF_03183; Endonuclease_III_Nth; 1.
InterPro; IPR011257; DNA_glycosylase.
InterPro; IPR004036; Endonuclease-III-like_CS2.
InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
InterPro; IPR003265; HhH-GPD_domain.
InterPro; IPR000445; HhH_motif.
InterPro; IPR023170; HTH_base_excis_C.
InterPro; IPR030841; NTH1.
Pfam; PF00633; HHH; 1.
Pfam; PF00730; HhH-GPD; 1.
SMART; SM00478; ENDO3c; 1.
SMART; SM00525; FES; 1.
SUPFAM; SSF48150; SSF48150; 1.
PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
1: Evidence at protein level;
4Fe-4S; Alternative initiation; Complete proteome;
Direct protein sequencing; DNA damage; DNA repair; Glycosidase;
Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; Mitochondrion;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transit peptide.
TRANSIT 1 30 Mitochondrion. {ECO:0000255|HAMAP-
Rule:MF_03183,
ECO:0000269|PubMed:12144783}.
CHAIN 31 312 Endonuclease III-like protein 1.
/FTId=PRO_0000102227.
DOMAIN 199 223 HhH. {ECO:0000255|HAMAP-Rule:MF_03183}.
MOTIF 36 60 Bipartite nuclear localization signal.
{ECO:0000255}.
ACT_SITE 220 220 Nucleophile; for N-glycosylase activity.
{ECO:0000255|HAMAP-Rule:MF_03183,
ECO:0000269|PubMed:9705289}.
METAL 290 290 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_03183}.
METAL 297 297 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_03183}.
METAL 300 300 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_03183}.
METAL 306 306 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
Rule:MF_03183}.
SITE 239 239 Important for catalytic activity.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VAR_SEQ 1 15 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_054292.
VAR_SEQ 1 8 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9045706,
ECO:0000303|PubMed:9705289,
ECO:0000303|PubMed:9831664}.
/FTId=VSP_054293.
VARIANT 21 21 R -> W (in dbSNP:rs3087469).
{ECO:0000269|Ref.3}.
/FTId=VAR_016125.
VARIANT 33 33 R -> K (in dbSNP:rs2302172).
/FTId=VAR_016126.
VARIANT 176 176 I -> T (in dbSNP:rs1805378).
/FTId=VAR_016127.
VARIANT 234 234 S -> L (in dbSNP:rs3211977).
{ECO:0000269|Ref.3}.
/FTId=VAR_029318.
VARIANT 239 239 D -> Y (in dbSNP:rs3087468).
/FTId=VAR_016128.
MUTAGEN 40 42 Missing: Sorted to the cytoplasm.
{ECO:0000269|PubMed:12531031}.
MUTAGEN 42 42 R->A: Sorted to both nuclei and
mitochondria.
{ECO:0000269|PubMed:12531031}.
MUTAGEN 42 42 R->D: Sorted to the cytoplasm.
{ECO:0000269|PubMed:12531031}.
MUTAGEN 57 57 R->A,D: Sorted to both nuclei and
mitochondria.
{ECO:0000269|PubMed:12531031}.
MUTAGEN 220 220 K->Q: Inactivates enzyme.
{ECO:0000269|PubMed:11695910,
ECO:0000269|PubMed:9705289}.
MUTAGEN 220 220 K->R: 85-fold reduction in activity.
Uncouples the glycosylase activity from
the lyase activity. Shows glycosylase
activity without any detectable AP-lyase
activity during the first 10 min of the
reaction. {ECO:0000269|PubMed:11695910,
ECO:0000269|PubMed:9705289}.
CONFLICT 9 10 MT -> TS (in Ref. 8; CAA70865).
{ECO:0000305}.
CONFLICT 78 78 Missing (in Ref. 8; CAA70865).
{ECO:0000305}.
CONFLICT 151 151 M -> I (in Ref. 1; AAB41534).
{ECO:0000305}.
CONFLICT 160 160 T -> A (in Ref. 1; AAB41534).
{ECO:0000305}.
SEQUENCE 312 AA; 34390 MW; 379816A1E0B45050 CRC64;
MCSPQESGMT ALSARMLTRS RSLGPGAGPR GCREEPGPLR RREAAAEARK SHSPVKRPRK
AQRLRVAYEG SDSEKGEGAE PLKVPVWEPQ DWQQQLVNIR AMRNKKDAPV DHLGTEHCYD
SSAPPKVRRY QVLLSLMLSS QTKDQVTAGA MQRLRARGLT VDSILQTDDA TLGKLIYPVG
FWRSKVKYIK QTSAILQQHY GGDIPASVAE LVALPGVGPK MAHLAMAVAW GTVSGIAVDT
HVHRIANRLR WTKKATKSPE ETRAALEEWL PRELWHEING LLVGFGQQTC LPVHPRCHAC
LNQALCPAAQ GL


Related products :

Catalog number Product name Quantity
EIAAB26876 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,Mouse,Mus musculus,NEH1,Nei homolog 1,Nei1,Neil1,Nei-like protein 1
EIAAB26879 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Homo sapiens,Human,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26878 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Gm1212,Mouse,Mus musculus,NEH2,Nei homolog 2,Neil2,Nei-like protein 2
EIAAB26880 Bos taurus,Bovine,DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26877 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,FPG1,Homo sapiens,Human,NEH1,Nei homolog 1,NEIL1,Nei-like protein 1
18-003-43422 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN; Protein REF-1 Polyclonal 0.1 mg Protein A
18-003-43959 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
18-003-43958 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
EH2009 DNA-(apurinic or apyrimidinic site) lyase Elisa Kit 96T
E14887d Mouse ELISA Kit FOR DNA-(apurinic or apyrimidinic site) lyase 2 96T
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase 500ug
AE56100RA Rat DNA- (apurinic or apyrimidinic site) lyase (APEX1) ELISA Kit 48T
CSB-EL001900RA Rat DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001901BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
abx108186 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (HRP) 100 μg
CSB-EL001900BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001900HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001901HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EL001901MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EL001900MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
abx109730 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody 100 μg
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase Source: E.coli 200ug
abx106767 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (FITC) 100 μg
abx105348 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (Biotin) 100 μg
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase Source: E.coli 1mg
Pathways :
WP1700: Selenoamino acid metabolism
WP1625: Base excision repair
WP1358: Selenium metabolism Selenoproteins
WP1705: Sulfur metabolism
WP1718: Vitamin B6 metabolism
WP28: Selenium Metabolism and Selenoproteins
WP390: Serine-isocitrate lyase pathway
WP108: Selenium metabolism/Selenoproteins
WP1293: Selenium metabolism Selenoproteins
WP668: Octadecanoid Pathway
WP1640: Cysteine and methionine metabolism
WP1030: Selenium metabolism Selenoproteins
WP1689: Porphyrin and chlorophyll metabolism
WP1149: Selenium metabolism Selenoproteins
WP1659: Glycine, serine and threonine metabolism
WP232: G Protein Signaling Pathways
WP1493: Carbon assimilation C4 pathway
WP1665: Limonene and pinene degradation
WP1675: Nitrogen metabolism
WP1566: Citrate cycle (TCA cycle)
WP1909: Signal regulatory protein (SIRP) family interactions
WP1624: Bacterial secretion system
WP210: Cytoplasmic Ribosomal Proteins
WP1685: Peptidoglycan biosynthesis
WP73: G Protein Signaling Pathways

Related Genes :
[NTHL1 NTH1 OCTS3] Endonuclease III-like protein 1 (hNTH1) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[nth-1 R10E4.5] Endonuclease III homolog (CeNTH) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[Nthl1 Nth1] Endonuclease III-like protein 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[NTH1 At2g31450 T28P16.6] Endonuclease III homolog 1, chloroplastic (AtNTH1) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1)
[NTG1 OGG2 SCR1 YAL015C FUN33] Endonuclease III homolog 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1) (Endonuclease III-like glycosylase 1) (Redoxyendonuclease 1)
[NTG2 SCR2 YOL043C] Endonuclease III homolog 2 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 2) (DNA glycosylase/AP lyase 2) (Endonuclease III-like glycosylase 2) (Redoxyendonuclease 2)
[NTH2 At1g05900 T20M3.18] Endonuclease III homolog 2, chloroplastic (AtNTH2) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 2) (DNA glycosylase/AP lyase 2)
[nth1 SPAC30D11.07] Endonuclease III homolog (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[Ogg1] N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]
[OGG1 MMH MUTM OGH1] N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]
[NEIL1] Endonuclease 8-like 1 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil1) (DNA-(apurinic or apyrimidinic site) lyase Neil1) (Endonuclease VIII-like 1) (FPG1) (Nei homolog 1) (NEH1) (Nei-like protein 1)
[OGG1 YML060W YM9958.02] N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]
[Ogg1 Mmh Ogh1] N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]
[Neil1 Nei1] Endonuclease 8-like 1 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil1) (DNA-(apurinic or apyrimidinic site) lyase Neil1) (Endonuclease VIII-like 1) (Nei homolog 1) (NEH1) (Nei-like protein 1)
[nei b0714 JW0704] Endonuclease 8 (DNA glycosylase/AP lyase Nei) (EC 3.2.2.-) (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site) lyase Nei) (Endonuclease VIII)
[] Endonuclease V (EC 3.2.2.17) (DNA-(apurinic or apyrimidinic site) lyase) (AP lyase) (EC 4.2.99.18) (T4 pyrimidine dimer glycosylase) (T4-Pdg)
[nei1 nei2 Rv2464c MTV008.20c] Endonuclease 8 1 (DNA glycosylase/AP lyase Nei 1) (EC 3.2.2.-) (DNA-(apurinic or apyrimidinic site) lyase Nei 1) (EC 4.2.99.18) (Endonuclease VIII 1)
[NEIL2] Endonuclease 8-like 2 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil2) (DNA-(apurinic or apyrimidinic site) lyase Neil2) (Endonuclease VIII-like 2) (Nei homolog 2) (NEH2) (Nei-like protein 2)
[mutM fpg] Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM) (AP lyase MutM) (EC 4.2.99.18)
[APEX1 APE APE1 APEX APX HAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[fpg1 mutM Rv2924c MTCY338.13c] Formamidopyrimidine-DNA glycosylase 1 (Fapy-DNA glycosylase 1) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM 1) (AP lyase MutM 1) (EC 4.2.99.18)
[mutM fpg b3635 JW3610] Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM) (AP lyase MutM) (EC 4.2.99.18)
[Neil2 Gm1212] Endonuclease 8-like 2 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil2) (DNA-(apurinic or apyrimidinic site) lyase Neil2) (Endonuclease VIII-like 2) (Nei homolog 2) (NEH2) (Nei-like protein 2)
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[FPG1 FPG2 At1g52500 F6D8.28] Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site) lyase FPG1) (Formamidopyrimidine-DNA glycosylase 1) (AtFPG-1) (Formamidopyrimidine-DNA glycosylase 2) (AtFPG-2) (Protein MutM homolog 1) (AtMMH-1) (Protein MutM homolog 2) (AtMMH-2)
[Apex2 Ape2] DNA-(apurinic or apyrimidinic site) lyase 2 (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease 2) (Apurinic-apyrimidinic endonuclease 2) (AP endonuclease 2)
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[PAE2237] N-glycosylase/DNA lyase (8-oxoguanine DNA glycosylase) (EC 3.2.2.-) (AGOG) (DNA-(apurinic or apyrimidinic site) lyase) (AP lyase) (EC 4.2.99.18) (Pa-AGOG)
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]

Bibliography :
No related Items