Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P78549 (NTH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endonuclease III-like protein 1

Short name=hNTH1
EC=3.2.2.-
EC=4.2.99.18
Alternative name(s):
Bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyase
Short name=DNA glycoslyase/AP lyase
Gene names
Name:NTHL1
Synonyms:NTH1, OCTS3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

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.

Cofactor

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 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.

Subunit structure

Interacts with YBX1.

Subcellular location

Nucleus. Mitochondrion Ref.16.

Tissue specificity

Widely expressed with highest levels in heart and lowest levels in lung and liver. Ref.1 Ref.2

Developmental stage

Expression levels are regulated during the cell cycle with increased levels during early and mid S-phase. Ref.8

Sequence similarities

Belongs to the Nth/MutY family.

Contains 1 HhH domain.

Biophysicochemical properties

Kinetic parameters:

KM=371 nM for 5-hydroxy-6-hydrothymine containing duplex oligonucleotides (N-glycosylase activity)

KM=1093 nM for 5-hydroxyuracil containing duplex oligonucleotides (N-glycosylase activity)

KM=548 nM for 5-hydroxycytosine containing duplex oligonucleotides (N-glycosylase activity)

KM=1101 nM for thymine glycol containing duplex oligonucleotides (N-glycosylase activity)

KM=718 nM for 5,6-dihydroxycytosine containing duplex oligonucleotides (N-glycosylase activity)

KM=0.05 nM for 5-hydroxycytosine-G containing duplex oligonucleotides (N-glycosylase activity)

KM=0.2 nM for 5-hydroxycytosine-A containing duplex oligonucleotides (N-glycosylase activity)

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentMitochondrion
Nucleus
   Coding sequence diversityAlternative initiation
Polymorphism
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionGlycosidase
Hydrolase
Lyase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay Ref.1. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

base-excision repair

Traceable author statement. Source: Reactome

base-excision repair, AP site formation

Inferred from direct assay PubMed 15358233. Source: UniProtKB

depyrimidination

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA incision, 5'-to lesion

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA N-glycosylase activity

Inferred from direct assay Ref.8. Source: UniProtKB

DNA-(apurinic or apyrimidinic site) lyase activity

Inferred from direct assay Ref.1. Source: UniProtKB

double-stranded DNA binding

Inferred from direct assay PubMed 15358233. Source: UniProtKB

endonuclease activity

Traceable author statement Ref.2. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 15358233. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P78549-1)

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.
Isoform 2 (identifier: P78549-2)

Also known as: M+1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.
Isoform 3 (identifier: P78549-3)

Also known as: M+8;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion
Chain31 – 312282Endonuclease III-like protein 1
PRO_0000102227

Regions

Domain199 – 22325HhH
Motif36 – 6025Bipartite nuclear localization signal Potential

Sites

Active site2201Nucleophile; for N-glycosylase activity Ref.5
Metal binding2901Iron-sulfur (4Fe-4S) By similarity UniProtKB P20625
Metal binding2971Iron-sulfur (4Fe-4S) By similarity UniProtKB P20625
Metal binding3001Iron-sulfur (4Fe-4S) By similarity UniProtKB P20625
Metal binding3061Iron-sulfur (4Fe-4S) By similarity UniProtKB P20625
Site2391Important for catalytic activity

Amino acid modifications

Modified residue711Phosphoserine
Modified residue731Phosphoserine

Natural variations

Alternative sequence1 – 1515Missing in isoform 3.
VSP_054292
Alternative sequence1 – 88Missing in isoform 2.
VSP_054293
Natural variant211R → W.
Corresponds to variant rs3087469 [ dbSNP | Ensembl ].
VAR_016125
Natural variant331R → K.
Corresponds to variant rs2302172 [ dbSNP | Ensembl ].
VAR_016126
Natural variant1761I → T.
Corresponds to variant rs1805378 [ dbSNP | Ensembl ].
VAR_016127
Natural variant2341S → L.
Corresponds to variant rs3211977 [ dbSNP | Ensembl ].
VAR_029318
Natural variant2391D → Y.
Corresponds to variant rs3087468 [ dbSNP | Ensembl ].
VAR_016128

Experimental info

Mutagenesis40 – 423Missing: Sorted to the cytoplasm.
Mutagenesis421R → A: Sorted to both nuclei and mitochondria.
Mutagenesis421R → D: Sorted to the cytoplasm.
Mutagenesis571R → A or D: Sorted to both nuclei and mitochondria.
Mutagenesis2201K → Q: Inactivates enzyme. Ref.5
Mutagenesis2201K → 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. Ref.5
Sequence conflict9 – 102MT → TS in CAA70865. Ref.8
Sequence conflict781Missing in CAA70865. Ref.8
Sequence conflict1511M → I in AAB41534. Ref.1
Sequence conflict1601T → A in AAB41534. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (M-8) [UniParc].

Last modified May 1, 1999. Version 2.
Checksum: 379816A1E0B45050

FASTA31234,390
        10         20         30         40         50         60 
MCSPQESGMT ALSARMLTRS RSLGPGAGPR GCREEPGPLR RREAAAEARK SHSPVKRPRK 

        70         80         90        100        110        120 
AQRLRVAYEG SDSEKGEGAE PLKVPVWEPQ DWQQQLVNIR AMRNKKDAPV DHLGTEHCYD 

       130        140        150        160        170        180 
SSAPPKVRRY QVLLSLMLSS QTKDQVTAGA MQRLRARGLT VDSILQTDDA TLGKLIYPVG 

       190        200        210        220        230        240 
FWRSKVKYIK QTSAILQQHY GGDIPASVAE LVALPGVGPK MAHLAMAVAW GTVSGIAVDT 

       250        260        270        280        290        300 
HVHRIANRLR WTKKATKSPE ETRAALEEWL PRELWHEING LLVGFGQQTC LPVHPRCHAC 

       310 
LNQALCPAAQ GL 

« Hide

Isoform 2 (M+1) [UniParc].

Checksum: DA97D508BE3D83F0
Show »

FASTA30433,570
Isoform 3 (M+8) [UniParc].

Checksum: 5D531E41F9F27975
Show »

FASTA29732,839

References

« Hide 'large scale' references
[1]"Cloning and characterization of a functional human homolog of Escherichia coli endonuclease III."
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.
Proc. Natl. Acad. Sci. U.S.A. 94:109-114(1997) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10457.1.
RefSeqNP_002519.1. NM_002528.5. [P78549-1]
UniGeneHs.66196.

3D structure databases

ProteinModelPortalP78549.
SMRP78549. Positions 130-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110968. 13 interactions.
STRING9606.ENSP00000219066.

PTM databases

PhosphoSiteP78549.

Polymorphism databases

DMDM29840795.

Proteomic databases

MaxQBP78549.
PaxDbP78549.
PRIDEP78549.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219066; ENSP00000219066; ENSG00000065057.
GeneID4913.
KEGGhsa:4913.
UCSCuc002col.1. human. [P78549-1]

Organism-specific databases

CTD4913.
GeneCardsGC16M002089.
HGNCHGNC:8028. NTHL1.
HPACAB025152.
MIM602656. gene.
neXtProtNX_P78549.
PharmGKBPA31811.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0177.
HOGENOMHOG000252209.
HOVERGENHBG052675.
InParanoidP78549.
KOK10773.
OMAWRNKVKY.
OrthoDBEOG76MK8Z.
PhylomeDBP78549.
TreeFamTF314967.

Enzyme and pathway databases

BRENDA4.2.99.18. 2681.
ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP78549.
BgeeP78549.
CleanExHS_NTHL1.
GenevestigatorP78549.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_03183. Endonuclease_III_Nth.
InterProIPR011257. 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]
PfamPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
PROSITEPS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNTHL1.
GenomeRNAi4913.
NextBio18903.
PROP78549.
SOURCESearch...

Entry information

Entry nameNTH_HUMAN
AccessionPrimary (citable) accession number: P78549
Secondary accession number(s): Q1MVR1 expand/collapse secondary AC list , Q99566, Q99794, Q9BPX2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM