Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96FI4

- NEIL1_HUMAN

UniProt

Q96FI4 - NEIL1_HUMAN

Protein

Endonuclease 8-like 1

Gene

NEIL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.4 Publications

    Catalytic activityi

    Removes damaged bases from DNA, leaving an abasic site.
    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.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21Schiff-base intermediate with DNACurated
    Active sitei3 – 31Proton donorCurated
    Active sitei54 – 541Proton donor; for beta-elimination activityCurated
    Binding sitei176 – 1761DNABy similarity
    Active sitei339 – 3391Proton donor; for delta-elimination activityCurated
    Binding sitei339 – 3391DNABy similarity

    GO - Molecular functioni

    1. damaged DNA binding Source: InterPro
    2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
    3. DNA N-glycosylase activity Source: Ensembl
    4. hydrolase activity, acting on glycosyl bonds Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. base-excision repair Source: UniProtKB
    2. negative regulation of nuclease activity Source: UniProtKB
    3. nucleotide-excision repair Source: InterPro
    4. response to oxidative stress Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BRENDAi3.2.2.23. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endonuclease 8-like 1 (EC:3.2.2.-, EC:4.2.99.18)
    Alternative name(s):
    DNA glycosylase/AP lyase Neil1
    DNA-(apurinic or apyrimidinic site) lyase Neil1
    Endonuclease VIII-like 1
    FPG1
    Nei homolog 1
    Short name:
    NEH1
    Nei-like protein 1
    Gene namesi
    Name:NEIL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:18448. NEIL1.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Nucleus 1 Publication. Chromosome 1 Publication
    Note: During mitosis, associates with centrosomes and condensed chromatin.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. microtubule organizing center Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21P → T: Loss of glycosylase and AP lyase activity. 2 Publications
    Mutagenesisi2 – 21Missing: Loss of glycosylase activity. 2 Publications
    Mutagenesisi3 – 31E → Q: Loss of glycosylase and AP lyase activity. 1 Publication
    Mutagenesisi54 – 541K → L: Loss of glycosylase activity. 1 Publication
    Mutagenesisi277 – 2771R → A: Strongly reduced glycosylase activity. Has little effect on AP lyase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA38334.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 390389Endonuclease 8-like 1PRO_0000170905Add
    BLAST

    Proteomic databases

    PaxDbiQ96FI4.
    PRIDEiQ96FI4.

    PTM databases

    PhosphoSiteiQ96FI4.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Inductioni

    Up-regulated during S-phase.1 Publication

    Gene expression databases

    ArrayExpressiQ96FI4.
    BgeeiQ96FI4.
    CleanExiHS_NEIL1.
    GenevestigatoriQ96FI4.

    Organism-specific databases

    HPAiHPA054084.

    Interactioni

    Protein-protein interaction databases

    BioGridi122787. 5 interactions.
    STRINGi9606.ENSP00000347170.

    Structurei

    Secondary structure

    1
    390
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1815
    Beta strandi23 – 264
    Beta strandi41 – 5212
    Beta strandi55 – 628
    Beta strandi73 – 786
    Turni80 – 823
    Beta strandi84 – 896
    Helixi90 – 923
    Beta strandi97 – 1037
    Beta strandi105 – 1084
    Beta strandi110 – 1156
    Beta strandi122 – 1276
    Turni137 – 1393
    Helixi141 – 15010
    Turni151 – 1533
    Helixi155 – 1584
    Helixi161 – 1644
    Turni168 – 1703
    Helixi176 – 18611
    Helixi194 – 1985
    Helixi199 – 2013
    Helixi212 – 2187
    Turni219 – 2213
    Helixi225 – 24016
    Helixi249 – 25911
    Beta strandi269 – 2724
    Beta strandi278 – 2836

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TDHX-ray2.10A1-390[»]
    4NRVX-ray2.60A2-290[»]
    ProteinModelPortaliQ96FI4.
    SMRiQ96FI4. Positions 2-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96FI4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FPG family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG75119.
    HOGENOMiHOG000067872.
    HOVERGENiHBG052592.
    InParanoidiQ96FI4.
    KOiK10567.
    OMAiHLASHFV.
    PhylomeDBiQ96FI4.
    TreeFamiTF333272.

    Family and domain databases

    InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
    IPR012319. DNA_glycosylase/AP_lyase_cat.
    IPR015371. Endonuclease-VIII_DNA-bd.
    IPR010979. Ribosomal_S13-like_H2TH.
    [Graphical view]
    PfamiPF01149. Fapy_DNA_glyco. 1 hit.
    PF06831. H2TH. 1 hit.
    PF09292. Neil1-DNA_bind. 1 hit.
    [Graphical view]
    SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
    [Graphical view]
    SUPFAMiSSF46946. SSF46946. 1 hit.
    SSF81624. SSF81624. 1 hit.
    PROSITEiPS51068. FPG_CAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q96FI4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEGPELHLA SQFVNEACRA LVFGGCVEKS SVSRNPEVPF ESSAYRISAS    50
    ARGKELRLIL SPLPGAQPQQ EPLALVFRFG MSGSFQLVPR EELPRHAHLR 100
    FYTAPPGPRL ALCFVDIRRF GRWDLGGKWQ PGRGPCVLQE YQQFRENVLR 150
    NLADKAFDRP ICEALLDQRF FNGIGNYLRA EILYRLKIPP FEKARSVLEA 200
    LQQHRPSPEL TLSQKIRTKL QNPDLLELCH SVPKEVVQLG GKGYGSESGE 250
    EDFAAFRAWL RCYGMPGMSS LQDRHGRTIW FQGDPGPLAP KGRKSRKKKS 300
    KATQLSPEDR VEDALPPSKA PSRTRRAKRD LPKRTATQRP EGTSLQQDPE 350
    APTVPKKGRR KGRQAASGHC RPRKVKADIP SLEPEGTSAS 390
    Length:390
    Mass (Da):43,684
    Last modified:January 23, 2007 - v3
    Checksum:iB2B058486C4EF835
    GO

    Sequence cautioni

    The sequence AK128372 differs from that shown. Reason: Erroneous CDS prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471N → S in BAB15337. (PubMed:14702039)Curated

    RNA editingi

    The edited form removes thymine glycol from duplex DNA 30 times more slowly than the form encoded in the genome, whereas editing enhances repair of the guanidinohydantoin lesion by NEIL1. The recoding site is a preferred editing site for the RNA editing adenosine deaminase ADAR1.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821S → C.1 Publication
    Corresponds to variant rs5745905 [ dbSNP | Ensembl ].
    VAR_020580
    Natural varianti83 – 831G → D.1 Publication
    Corresponds to variant rs5745906 [ dbSNP | Ensembl ].
    VAR_020581
    Natural varianti136 – 1361C → R.1 Publication
    Corresponds to variant rs5745907 [ dbSNP | Ensembl ].
    VAR_020582
    Natural varianti159 – 1591R → Q.1 Publication
    VAR_065963
    Natural varianti181 – 1811E → K Found in a patient with nephrotic syndrome also carrying mutation P-159 in MYO1E. 1 Publication
    VAR_065964
    Natural varianti182 – 1821I → M.
    Corresponds to variant rs7183491 [ dbSNP | Ensembl ].
    VAR_020583
    Natural varianti242 – 2421K → R in RNA edited version.
    VAR_065018
    Natural varianti252 – 2521D → N.1 Publication
    Corresponds to variant rs5745926 [ dbSNP | Ensembl ].
    VAR_020584

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079068 mRNA. Translation: BAC06476.1.
    AK026055 mRNA. Translation: BAB15337.1.
    AK128372 mRNA. No translation available.
    AY257544 Genomic DNA. Translation: AAO74826.1.
    AC068338 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99255.1.
    CH471136 Genomic DNA. Translation: EAW99260.1.
    BC010876 mRNA. Translation: AAH10876.1.
    CCDSiCCDS10278.1.
    RefSeqiNP_001243481.1. NM_001256552.1.
    NP_078884.2. NM_024608.3.
    XP_005254716.1. XM_005254659.2.
    XP_006720743.1. XM_006720680.1.
    XP_006720744.1. XM_006720681.1.
    XP_006720745.1. XM_006720682.1.
    UniGeneiHs.512732.

    Genome annotation databases

    EnsembliENST00000355059; ENSP00000347170; ENSG00000140398.
    ENST00000564784; ENSP00000457352; ENSG00000140398.
    ENST00000569035; ENSP00000455730; ENSG00000140398.
    GeneIDi79661.
    KEGGihsa:79661.
    UCSCiuc002bad.4. human.

    Polymorphism databases

    DMDMi56404654.

    Keywords - Coding sequence diversityi

    Polymorphism, RNA editing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079068 mRNA. Translation: BAC06476.1 .
    AK026055 mRNA. Translation: BAB15337.1 .
    AK128372 mRNA. No translation available.
    AY257544 Genomic DNA. Translation: AAO74826.1 .
    AC068338 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99255.1 .
    CH471136 Genomic DNA. Translation: EAW99260.1 .
    BC010876 mRNA. Translation: AAH10876.1 .
    CCDSi CCDS10278.1.
    RefSeqi NP_001243481.1. NM_001256552.1.
    NP_078884.2. NM_024608.3.
    XP_005254716.1. XM_005254659.2.
    XP_006720743.1. XM_006720680.1.
    XP_006720744.1. XM_006720681.1.
    XP_006720745.1. XM_006720682.1.
    UniGenei Hs.512732.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TDH X-ray 2.10 A 1-390 [» ]
    4NRV X-ray 2.60 A 2-290 [» ]
    ProteinModelPortali Q96FI4.
    SMRi Q96FI4. Positions 2-290.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122787. 5 interactions.
    STRINGi 9606.ENSP00000347170.

    PTM databases

    PhosphoSitei Q96FI4.

    Polymorphism databases

    DMDMi 56404654.

    Proteomic databases

    PaxDbi Q96FI4.
    PRIDEi Q96FI4.

    Protocols and materials databases

    DNASUi 79661.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355059 ; ENSP00000347170 ; ENSG00000140398 .
    ENST00000564784 ; ENSP00000457352 ; ENSG00000140398 .
    ENST00000569035 ; ENSP00000455730 ; ENSG00000140398 .
    GeneIDi 79661.
    KEGGi hsa:79661.
    UCSCi uc002bad.4. human.

    Organism-specific databases

    CTDi 79661.
    GeneCardsi GC15P075639.
    H-InvDB HIX0202149.
    HGNCi HGNC:18448. NEIL1.
    HPAi HPA054084.
    MIMi 608844. gene.
    neXtProti NX_Q96FI4.
    PharmGKBi PA38334.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG75119.
    HOGENOMi HOG000067872.
    HOVERGENi HBG052592.
    InParanoidi Q96FI4.
    KOi K10567.
    OMAi HLASHFV.
    PhylomeDBi Q96FI4.
    TreeFami TF333272.

    Enzyme and pathway databases

    BRENDAi 3.2.2.23. 2681.

    Miscellaneous databases

    EvolutionaryTracei Q96FI4.
    GeneWikii NEIL1.
    GenomeRNAii 79661.
    NextBioi 68852.
    PROi Q96FI4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96FI4.
    Bgeei Q96FI4.
    CleanExi HS_NEIL1.
    Genevestigatori Q96FI4.

    Family and domain databases

    InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
    IPR012319. DNA_glycosylase/AP_lyase_cat.
    IPR015371. Endonuclease-VIII_DNA-bd.
    IPR010979. Ribosomal_S13-like_H2TH.
    [Graphical view ]
    Pfami PF01149. Fapy_DNA_glyco. 1 hit.
    PF06831. H2TH. 1 hit.
    PF09292. Neil1-DNA_bind. 1 hit.
    [Graphical view ]
    SMARTi SM00898. Fapy_DNA_glyco. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46946. SSF46946. 1 hit.
    SSF81624. SSF81624. 1 hit.
    PROSITEi PS51068. FPG_CAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A back-up glycosylase in Nth1 knock-out mice is a functional Nei (endonuclease VIII) homologue."
      Takao M., Kanno S., Kobayashi K., Zhang Q.-M., Yonei S., van der Horst G.T.J., Yasui A.
      J. Biol. Chem. 277:42205-42213(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Testis.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. NIEHS SNPs program
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-82; ASP-83; ARG-136 AND ASN-252.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Lung.
    7. "A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII."
      Bandaru V., Sunkara S., Wallace S.S., Bond J.P.
      DNA Repair 1:517-529(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-2 AND GLU-3, FUNCTION.
    8. "Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA."
      Hazra T.K., Izumi T., Boldogh I., Imhoff B., Kow Y.W., Jaruga P., Dizdaroglu M., Mitra S.
      Proc. Natl. Acad. Sci. U.S.A. 99:3523-3528(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-2, FUNCTION, INDUCTION, TISSUE SPECIFICITY.
    9. "Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2."
      Dou H., Mitra S., Hazra T.K.
      J. Biol. Chem. 278:49679-49684(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-54.
    10. "Human NEIL1 localizes with the centrosomes and condensed chromosomes during mitosis."
      Hildrestrand G.A., Rolseth V., Bjoras M., Luna L.
      DNA Repair 6:1425-1433(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "RNA editing changes the lesion specificity for the DNA repair enzyme NEIL1."
      Yeo J., Goodman R.A., Schirle N.T., David S.S., Beal P.A.
      Proc. Natl. Acad. Sci. U.S.A. 107:20715-20719(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA EDITING OF POSITION 242.
    12. "The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity."
      Doublie S., Bandaru V., Bond J.P., Wallace S.S.
      Proc. Natl. Acad. Sci. U.S.A. 101:10284-10289(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-334, MUTAGENESIS OF ARG-277.
    13. Cited for: VARIANTS GLN-159 AND LYS-181.

    Entry informationi

    Entry nameiNEIL1_HUMAN
    AccessioniPrimary (citable) accession number: Q96FI4
    Secondary accession number(s): D3DW75
    , Q6ZRA7, Q86XW7, Q9H6C3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 123 of the entry and version 3 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

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3