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
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.UniRule annotation1 Publication

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.UniRule annotationBy similarity

Cofactori

[4Fe-4S] clusterUniRule annotationNote: 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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei208 – 2081Nucleophile; for N-glycosylase activityUniRule annotation
Sitei227 – 2271Important for catalytic activityUniRule annotation
Metal bindingi278 – 2781Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi285 – 2851Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi288 – 2881Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi294 – 2941Iron-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: MGI
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. base-excision repair, AP site formation Source: MGI
  2. DNA catabolic process, endonucleolytic Source: MGI
  3. DNA repair Source: MGI
  4. 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. 3474.
ReactomeiREACT_208690. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
REACT_220827. Displacement of DNA glycosylase by APE1.

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease III-like protein 1UniRule annotation (EC:3.2.2.-UniRule annotation, EC:4.2.99.18UniRule annotation)
Alternative name(s):
Bifunctional DNA N-glycoslyase/DNA-(apurinic or apyrimidinic site) lyaseUniRule annotation
Short name:
DNA glycoslyase/AP lyaseUniRule annotation
Gene namesi
Name:Nthl1
Synonyms:Nth1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1313275. Nthl1.

Subcellular locationi

Nucleus UniRule annotation. Mitochondrion UniRule annotation1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionUniRule annotationAdd
BLAST
Chaini20 – 300281Endonuclease III-like protein 1PRO_0000102228Add
BLAST

Proteomic databases

PRIDEiO35980.

PTM databases

PhosphoSiteiO35980.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

CleanExiMM_NTHL1.
GenevestigatoriO35980.

Interactioni

Subunit structurei

Interacts with YBX1.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliO35980.
SMRiO35980. Positions 105-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini187 – 21125HhHUniRule annotationAdd
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.
InParanoidiO35980.
KOiK10773.
OMAiWRNKVKY.
OrthoDBiEOG76MK8Z.
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]

Sequencei

Sequence statusi: Complete.

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

O35980-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSGVRMVTR SRSRATRIAS EGCREELAPR EAAAEGRKSH RPVRHPRRTQ
60 70 80 90 100
KTHVAYEAAN GEEGEDAEPL KVPVWEPQNW QQQLANIRIM RSKKDAPVDQ
110 120 130 140 150
LGAEHCYDAS ASPKVRRYQV LLSLMLSSQT KDQVTAGAMQ RLRARGLTVE
160 170 180 190 200
SILQTDDDTL GRLIYPVGFW RNKVKYIKQT TAILQQRYEG DIPASVAELV
210 220 230 240 250
ALPGVGPKMA HLAMAVAWGT ISGIAVDTHV HRIANRLRWT KKMTKTPEET
260 270 280 290 300
RKNLEEWLPR VLWSEVNGLL VGFGQQICLP VHPRCQACLN KALCPAAQDL
Length:300
Mass (Da):33,637
Last modified:April 16, 2014 - v2
Checksum:i09CAA1FD066F18EB
GO

Sequence cautioni

The sequence AK033701 differs from that shown. Reason: Frameshift at position 33. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006812 mRNA. Translation: BAA22080.1.
AB009371 Genomic DNA. Translation: BAA28846.1.
AJ001617 Genomic DNA. Translation: CAB65239.1.
Y09688 mRNA. Translation: CAA70866.1.
AK033701 mRNA. No translation available.
AC132367 Genomic DNA. No translation available.
CCDSiCCDS28487.1.
RefSeqiNP_032769.2. NM_008743.2.
UniGeneiMm.148315.

Genome annotation databases

EnsembliENSMUST00000047611; ENSMUSP00000047413; ENSMUSG00000041429.
GeneIDi18207.
KEGGimmu:18207.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006812 mRNA. Translation: BAA22080.1.
AB009371 Genomic DNA. Translation: BAA28846.1.
AJ001617 Genomic DNA. Translation: CAB65239.1.
Y09688 mRNA. Translation: CAA70866.1.
AK033701 mRNA. No translation available.
AC132367 Genomic DNA. No translation available.
CCDSiCCDS28487.1.
RefSeqiNP_032769.2. NM_008743.2.
UniGeneiMm.148315.

3D structure databases

ProteinModelPortaliO35980.
SMRiO35980. Positions 105-294.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiO35980.

Proteomic databases

PRIDEiO35980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047611; ENSMUSP00000047413; ENSMUSG00000041429.
GeneIDi18207.
KEGGimmu:18207.

Organism-specific databases

CTDi4913.
MGIiMGI:1313275. Nthl1.

Phylogenomic databases

eggNOGiCOG0177.
GeneTreeiENSGT00510000047513.
HOGENOMiHOG000252209.
HOVERGENiHBG052675.
InParanoidiO35980.
KOiK10773.
OMAiWRNKVKY.
OrthoDBiEOG76MK8Z.
TreeFamiTF314967.

Enzyme and pathway databases

BRENDAi4.2.99.18. 3474.
ReactomeiREACT_208690. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
REACT_220827. Displacement of DNA glycosylase by APE1.

Miscellaneous databases

ChiTaRSiNthl1. mouse.
NextBioi293586.
PROiO35980.
SOURCEiSearch...

Gene expression databases

CleanExiMM_NTHL1.
GenevestigatoriO35980.

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. "Cloning and characterization of a mouse homologue (mNthl1) of Escherichia coli endonuclease III."
    Sarker A.H., Ikeda S., Nakano H., Terato H., Ide H., Imai K., Akiyama K., Tsutsui K., Bo Z., Kubo K., Yamamoto K., Yasui A., Yoshida M.C., Seki S.
    J. Mol. Biol. 282:761-774(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Leukocyte and T-cell.
  2. "Complete genomic DNA sequence of the Mus musculus endonuclease III homologue 1 gene (NTH1)."
    Luna L., Bjoras M., Rognes T., Hoff E., Seeberg E.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Embryonic stem cell and Lung.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cecum.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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.

Entry informationi

Entry nameiNTH_MOUSE
AccessioniPrimary (citable) accession number: O35980
Secondary accession number(s): E9QMW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: April 16, 2014
Last modified: February 4, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.