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O35980

- NTH_MOUSE

UniProt

O35980 - NTH_MOUSE

Protein

Endonuclease III-like protein 1

Gene

Nthl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (16 Apr 2014)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    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 similarityUniRule annotation

    Cofactori

    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 binding Source: InterPro
    4. DNA N-glycosylase activity Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. base-excision repair Source: InterPro
    2. DNA catabolic process, endonucleolytic Source: GOC
    3. DNA repair Source: MGI
    4. nucleotide-excision repair, DNA incision, 5'-to lesion Source: UniProtKB

    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: Unplaced

    Organism-specific databases

    MGIiMGI:1313275. Nthl1.

    Subcellular locationi

    Nucleus UniRule annotation. Mitochondrion 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB
    2. nucleus Source: MGI

    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.
    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

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    MNSGVRMVTR SRSRATRIAS EGCREELAPR EAAAEGRKSH RPVRHPRRTQ    50
    KTHVAYEAAN GEEGEDAEPL KVPVWEPQNW QQQLANIRIM RSKKDAPVDQ 100
    LGAEHCYDAS ASPKVRRYQV LLSLMLSSQT KDQVTAGAMQ RLRARGLTVE 150
    SILQTDDDTL GRLIYPVGFW RNKVKYIKQT TAILQQRYEG DIPASVAELV 200
    ALPGVGPKMA HLAMAVAWGT ISGIAVDTHV HRIANRLRWT KKMTKTPEET 250
    RKNLEEWLPR VLWSEVNGLL VGFGQQICLP VHPRCQACLN KALCPAAQDL 300
    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS28487.1.
    RefSeqi NP_032769.2. NM_008743.2.
    UniGenei Mm.148315.

    3D structure databases

    ProteinModelPortali O35980.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei O35980.

    Proteomic databases

    PRIDEi O35980.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000047611 ; ENSMUSP00000047413 ; ENSMUSG00000041429 .
    GeneIDi 18207.
    KEGGi mmu:18207.

    Organism-specific databases

    CTDi 4913.
    MGIi MGI:1313275. Nthl1.

    Phylogenomic databases

    eggNOGi COG0177.
    GeneTreei ENSGT00510000047513.
    HOGENOMi HOG000252209.
    HOVERGENi HBG052675.
    InParanoidi O35980.
    KOi K10773.
    OMAi WRNKVKY.
    OrthoDBi EOG76MK8Z.
    TreeFami TF314967.

    Enzyme and pathway databases

    BRENDAi 4.2.99.18. 3474.
    Reactomei REACT_208690. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
    REACT_220827. Displacement of DNA glycosylase by APE1.

    Miscellaneous databases

    ChiTaRSi NTHL1. mouse.
    NextBioi 293586.
    PROi O35980.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_NTHL1.
    Genevestigatori O35980.

    Family and domain databases

    Gene3Di 1.10.1670.10. 1 hit.
    1.10.340.30. 1 hit.
    HAMAPi MF_03183. Endonuclease_III_Nth.
    InterProi IPR011257. 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 ]
    Pfami PF00633. HHH. 1 hit.
    PF00730. HhH-GPD. 1 hit.
    [Graphical view ]
    SMARTi SM00478. ENDO3c. 1 hit.
    SM00525. FES. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48150. SSF48150. 1 hit.
    PROSITEi PS01155. ENDONUCLEASE_III_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 114 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