Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endonuclease III-like protein 1

Gene

NTHL1

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

Functioni

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.17 Publications

Catalytic activityi

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.By similarity3 PublicationsUniRule annotation

Cofactori

[4Fe-4S] clusterNote: 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.

Enzyme regulationi

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 YBX1.2 Publications

Kineticsi

  1. KM=371 nM for 5-hydroxy-6-hydrothymine containing duplex oligonucleotides (N-glycosylase activity)2 Publications
  2. KM=1093 nM for 5-hydroxyuracil containing duplex oligonucleotides (N-glycosylase activity)2 Publications
  3. KM=548 nM for 5-hydroxycytosine containing duplex oligonucleotides (N-glycosylase activity)2 Publications
  4. KM=1101 nM for thymine glycol containing duplex oligonucleotides (N-glycosylase activity)2 Publications
  5. KM=718 nM for 5,6-dihydroxycytosine containing duplex oligonucleotides (N-glycosylase activity)2 Publications
  6. KM=0.05 nM for 5-hydroxycytosine-G containing duplex oligonucleotides (N-glycosylase activity)2 Publications
  7. KM=0.2 nM for 5-hydroxycytosine-A containing duplex oligonucleotides (N-glycosylase activity)2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei220 – 2201Nucleophile; for N-glycosylase activity1 PublicationUniRule annotation
Sitei239 – 2391Important for catalytic activity
Metal bindingi290 – 2901Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi297 – 2971Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi300 – 3001Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi306 – 3061Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
  3. DNA N-glycosylase activity Source: UniProtKB
  4. double-stranded DNA binding Source: UniProtKB
  5. endonuclease activity Source: ProtInc
  6. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. base-excision repair Source: Reactome
  2. base-excision repair, AP site formation Source: UniProtKB
  3. depyrimidination Source: Reactome
  4. DNA catabolic process, endonucleolytic Source: GOC
  5. DNA repair Source: Reactome
  6. nucleotide-excision repair, DNA incision, 5'-to lesion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.99.18. 2681.
ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease III-like protein 1UniRule annotation (EC:3.2.2.-UniRule annotation, EC:4.2.99.18UniRule annotation)
Short name:
hNTH1
Alternative name(s):
Bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyaseUniRule annotation
Short name:
DNA glycoslyase/AP lyaseUniRule annotation
Gene namesi
Name:NTHL1UniRule annotation
Synonyms:NTH1, OCTS3
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:8028. NTHL1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 423Missing: Sorted to the cytoplasm. 1 Publication
Mutagenesisi42 – 421R → A: Sorted to both nuclei and mitochondria. 1 Publication
Mutagenesisi42 – 421R → D: Sorted to the cytoplasm. 1 Publication
Mutagenesisi57 – 571R → A or D: Sorted to both nuclei and mitochondria. 1 Publication
Mutagenesisi220 – 2201K → Q: Inactivates enzyme. 2 Publications
Mutagenesisi220 – 2201K → 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. 2 Publications

Organism-specific databases

PharmGKBiPA31811.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion1 PublicationUniRule annotationAdd
BLAST
Chaini31 – 312282Endonuclease III-like protein 1PRO_0000102227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711Phosphoserine2 Publications
Modified residuei73 – 731Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78549.
PaxDbiP78549.
PRIDEiP78549.

PTM databases

PhosphoSiteiP78549.

Expressioni

Tissue specificityi

Widely expressed with highest levels in heart and lowest levels in lung and liver.2 Publications

Developmental stagei

Expression levels are regulated during the cell cycle with increased levels during early and mid S-phase.1 Publication

Gene expression databases

BgeeiP78549.
CleanExiHS_NTHL1.
ExpressionAtlasiP78549. baseline and differential.
GenevestigatoriP78549.

Organism-specific databases

HPAiCAB025152.

Interactioni

Subunit structurei

Interacts with YBX1.1 PublicationUniRule annotation

Protein-protein interaction databases

BioGridi110968. 14 interactions.
STRINGi9606.ENSP00000219066.

Structurei

3D structure databases

ProteinModelPortaliP78549.
SMRiP78549. Positions 130-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini199 – 22325HhHUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 6025Bipartite nuclear localization signalSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the Nth/MutY family.UniRule annotation
Contains 1 HhH domain.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0177.
GeneTreeiENSGT00510000047513.
HOGENOMiHOG000252209.
HOVERGENiHBG052675.
InParanoidiP78549.
KOiK10773.
OMAiWRNKVKY.
OrthoDBiEOG76MK8Z.
PhylomeDBiP78549.
TreeFamiTF314967.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPiMF_03183. Endonuclease_III_Nth.
InterProiIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
PROSITEiPS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P78549-1) [UniParc]FASTAAdd to Basket

Also known as: M-8

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCSPQESGMT ALSARMLTRS RSLGPGAGPR GCREEPGPLR RREAAAEARK
60 70 80 90 100
SHSPVKRPRK AQRLRVAYEG SDSEKGEGAE PLKVPVWEPQ DWQQQLVNIR
110 120 130 140 150
AMRNKKDAPV DHLGTEHCYD SSAPPKVRRY QVLLSLMLSS QTKDQVTAGA
160 170 180 190 200
MQRLRARGLT VDSILQTDDA TLGKLIYPVG FWRSKVKYIK QTSAILQQHY
210 220 230 240 250
GGDIPASVAE LVALPGVGPK MAHLAMAVAW GTVSGIAVDT HVHRIANRLR
260 270 280 290 300
WTKKATKSPE ETRAALEEWL PRELWHEING LLVGFGQQTC LPVHPRCHAC
310
LNQALCPAAQ GL
Length:312
Mass (Da):34,390
Last modified:May 1, 1999 - v2
Checksum:i379816A1E0B45050
GO
Isoform 2 (identifier: P78549-2) [UniParc]FASTAAdd to Basket

Also known as: M+1

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.

Show »
Length:304
Mass (Da):33,570
Checksum:iDA97D508BE3D83F0
GO
Isoform 3 (identifier: P78549-3) [UniParc]FASTAAdd to Basket

Also known as: M+8

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: Missing.

Show »
Length:297
Mass (Da):32,839
Checksum:i5D531E41F9F27975
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 102MT → TS in CAA70865. (PubMed:10882850)Curated
Sequence conflicti78 – 781Missing in CAA70865. (PubMed:10882850)Curated
Sequence conflicti151 – 1511M → I in AAB41534. (PubMed:8990169)Curated
Sequence conflicti160 – 1601T → A in AAB41534. (PubMed:8990169)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211R → W.1 Publication
Corresponds to variant rs3087469 [ dbSNP | Ensembl ].
VAR_016125
Natural varianti33 – 331R → K.
Corresponds to variant rs2302172 [ dbSNP | Ensembl ].
VAR_016126
Natural varianti176 – 1761I → T.
Corresponds to variant rs1805378 [ dbSNP | Ensembl ].
VAR_016127
Natural varianti234 – 2341S → L.1 Publication
Corresponds to variant rs3211977 [ dbSNP | Ensembl ].
VAR_029318
Natural varianti239 – 2391D → Y.
Corresponds to variant rs3087468 [ dbSNP | Ensembl ].
VAR_016128

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515Missing in isoform 3. CuratedVSP_054292Add
BLAST
Alternative sequencei1 – 88Missing in isoform 2. 4 PublicationsVSP_054293

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79718 mRNA. Translation: AAB41534.1.
AB014460 Genomic DNA. Translation: BAA32695.1.
AF498098 Genomic DNA. Translation: AAM11786.1.
AC005600 Genomic DNA. Translation: AAC34209.1.
AB001575 mRNA. Translation: BAA19413.1.
U81285 mRNA. Translation: AAC51136.1.
BC003014 mRNA. Translation: AAH03014.1.
BC000391 mRNA. Translation: AAH00391.2.
Y09687 mRNA. Translation: CAA70865.1.
CCDSiCCDS10457.1. [P78549-1]
RefSeqiNP_002519.1. NM_002528.5. [P78549-1]
UniGeneiHs.66196.

Genome annotation databases

GeneIDi4913.
KEGGihsa:4913.
UCSCiuc002col.1. human. [P78549-1]

Polymorphism databases

DMDMi29840795.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79718 mRNA. Translation: AAB41534.1.
AB014460 Genomic DNA. Translation: BAA32695.1.
AF498098 Genomic DNA. Translation: AAM11786.1.
AC005600 Genomic DNA. Translation: AAC34209.1.
AB001575 mRNA. Translation: BAA19413.1.
U81285 mRNA. Translation: AAC51136.1.
BC003014 mRNA. Translation: AAH03014.1.
BC000391 mRNA. Translation: AAH00391.2.
Y09687 mRNA. Translation: CAA70865.1.
CCDSiCCDS10457.1. [P78549-1]
RefSeqiNP_002519.1. NM_002528.5. [P78549-1]
UniGeneiHs.66196.

3D structure databases

ProteinModelPortaliP78549.
SMRiP78549. Positions 130-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110968. 14 interactions.
STRINGi9606.ENSP00000219066.

PTM databases

PhosphoSiteiP78549.

Polymorphism databases

DMDMi29840795.

Proteomic databases

MaxQBiP78549.
PaxDbiP78549.
PRIDEiP78549.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4913.
KEGGihsa:4913.
UCSCiuc002col.1. human. [P78549-1]

Organism-specific databases

CTDi4913.
GeneCardsiGC16M002089.
HGNCiHGNC:8028. NTHL1.
HPAiCAB025152.
MIMi602656. gene.
neXtProtiNX_P78549.
PharmGKBiPA31811.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0177.
GeneTreeiENSGT00510000047513.
HOGENOMiHOG000252209.
HOVERGENiHBG052675.
InParanoidiP78549.
KOiK10773.
OMAiWRNKVKY.
OrthoDBiEOG76MK8Z.
PhylomeDBiP78549.
TreeFamiTF314967.

Enzyme and pathway databases

BRENDAi4.2.99.18. 2681.
ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.

Miscellaneous databases

GeneWikiiNTHL1.
GenomeRNAii4913.
NextBioi18903.
PROiP78549.
SOURCEiSearch...

Gene expression databases

BgeeiP78549.
CleanExiHS_NTHL1.
ExpressionAtlasiP78549. baseline and differential.
GenevestigatoriP78549.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPiMF_03183. Endonuclease_III_Nth.
InterProiIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
PROSITEiPS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. "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."
    Imai K., Sarker A.H., Akiyama K., Ikeda S., Yao M., Tsutsui K., Shohmori T., Seki S.
    Gene 222:287-295(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Placenta.
  3. NIEHS SNPs program
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-21 AND LEU-234.
  4. "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].
  5. "Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue."
    Ikeda S., Biswas T., Roy R., Izumi T., Boldogh I., Kurosky A., Sarker A.H., Seki S., Mitra S.
    J. Biol. Chem. 273:21585-21593(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ACTIVE SITE, MUTAGENESIS OF LYS-220.
    Tissue: Bone marrow.
  6. "Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III."
    Hilbert T.P., Chaung W., Boorstein R.J., Cunningham R.P., Teebor G.W.
    J. Biol. Chem. 272:6733-6740(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
    Tissue: Spleen.
  7. "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] OF 8-312 (ISOFORMS 1 AND 2).
    Tissue: Lung.
  8. "Cell-cycle regulation, intracellular sorting and induced overexpression of the human NTH1 DNA glycosylase involved in removal of formamidopyrimidine residues from DNA."
    Luna L., Bjoras M., Hoff E., Rognes T., Seeberg E.
    Mutat. Res. 460:95-104(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-312, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  9. "Truncation of amino-terminal tail stimulates activity of human endonuclease III (hNTH1)."
    Liu X., Roy R.
    J. Mol. Biol. 321:265-276(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-37; 48-56; 61-78; 107-113; 120-126 AND 221-227, FUNCTION, CATALYTIC ACTIVITY.
  10. "Mitochondrial targeting of human DNA glycosylases for repair of oxidative DNA damage."
    Takao M., Aburatani H., Kobayashi K., Yasui A.
    Nucleic Acids Res. 26:2917-2922(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Excision of products of oxidative DNA base damage by human NTH1 protein."
    Dizdaroglu M., Karahalil B., Senturker S., Buckley T.J., Roldan-Arjona T.
    Biochemistry 38:243-246(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  12. "Human endonuclease III acts preferentially on DNA damage opposite guanine residues in DNA."
    Eide L., Luna L., Gustad E.C., Henderson P.T., Essigmann J.M., Demple B., Seeberg E.
    Biochemistry 40:6653-6659(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  13. "Mutation at active site lysine 212 to arginine uncouples the glycosylase activity from the lyase activity of human endonuclease III."
    Liu X., Roy R.
    Biochemistry 40:13617-13622(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-220.
  14. "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."
    Marenstein D.R., Ocampo M.T., Chan M.K., Altamirano A., Basu A.K., Boorstein R.J., Cunningham R.P., Teebor G.W.
    J. Biol. Chem. 276:21242-21249(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, INTERACTION WITH YBX1, ENZYME REGULATION.
  15. "Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA."
    Matsumoto Y., Zhang Q.M., Takao M., Yasui A., Yonei S.
    Nucleic Acids Res. 29:1975-1981(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Differential intracellular localization of the human and mouse endonuclease III homologs and analysis of the sorting signals."
    Ikeda S., Kohmoto T., Tabata R., Seki Y.
    DNA Repair 1:847-854(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, MUTAGENESIS OF 40-ARG--ARG-42; ARG-42 AND ARG-57.
  17. "Identification of 5-formyluracil DNA glycosylase activity of human hNTH1 protein."
    Miyabe I., Zhang Q.M., Kino K., Sugiyama H., Takao M., Yasui A., Yonei S.
    Nucleic Acids Res. 30:3443-3448(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  18. "Substrate specificity of human endonuclease III (hNTH1). Effect of human APE1 on hNTH1 activity."
    Marenstein D.R., Chan M.K., Altamirano A., Basu A.K., Boorstein R.J., Cunningham R.P., Teebor G.W.
    J. Biol. Chem. 278:9005-9012(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATES, ENZYME REGULATION.
  19. "Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions."
    Katafuchi A., Nakano T., Masaoka A., Terato H., Iwai S., Hanaoka F., Ide H.
    J. Biol. Chem. 279:14464-14471(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATES.
  20. "DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells."
    Zhang Q.M., Yonekura S., Takao M., Yasui A., Sugiyama H., Yonei S.
    DNA Repair 4:71-79(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATES.
  21. "Initiation of base excision repair of oxidative lesions in nucleosomes by the human, bifunctional DNA glycosylase NTH1."
    Prasad A., Wallace S.S., Pederson D.S.
    Mol. Cell. Biol. 27:8442-8453(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "Non-specific DNA binding interferes with the efficient excision of oxidative lesions from chromatin by the human DNA glycosylase, NEIL1."
    Odell I.D., Newick K., Heintz N.H., Wallace S.S., Pederson D.S.
    DNA Repair 9:134-143(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "Fluorescent probes for the analysis of DNA strand scission in base excision repair."
    Matsumoto N., Toga T., Hayashi R., Sugasawa K., Katayanagi K., Ide H., Kuraoka I., Iwai S.
    Nucleic Acids Res. 38:E101-E101(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Nucleosome disruption by DNA ligase III-XRCC1 promotes efficient base excision repair."
    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.
    Mol. Cell. Biol. 31:4623-4632(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNTH_HUMAN
AccessioniPrimary (citable) accession number: P78549
Secondary accession number(s): Q1MVR1
, Q99566, Q99794, Q9BPX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 141 of the entry and version 2 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

Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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