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Q8TAT5

- NEIL3_HUMAN

UniProt

Q8TAT5 - NEIL3_HUMAN

Protein

Endonuclease 8-like 3

Gene

NEIL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (10 Aug 2010)
      Previous versions | rss
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    Functioni

    DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). In vitro, displays strong glycosylase activity towards the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in both ssDNA and dsDNA; also recognizes FapyA, FapyG, 5-OHU, 5-OHC, 5-OHMH, Tg and 8-oxoA lesions in ssDNA. No activity on 8-oxoG detected. Also shows weak DNA-(apurinic or apyrimidinic site) lyase activity. In vivo, appears to be the primary enzyme involved in removing Sp and Gh from ssDNA in neonatal tissues. Seems to be an important facilitator of cell proliferation in certain populations, for example neural stem/progenitor cells and tumor cells, suggesting a role in replication-associated DNA repair.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 DNA; via amino nitrogenPROSITE-ProRule annotation
    Sitei2 – 21Important for monofunctional glycosylase activity
    Sitei81 – 811Required for glycosylase and lyase activities
    Binding sitei192 – 1921DNABy similarity
    Binding sitei271 – 2711DNABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri247 – 28135FPG-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri317 – 34630RanBP2-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. bubble DNA binding Source: UniProtKB
    2. damaged DNA binding Source: InterPro
    3. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
    4. DNA N-glycosylase activity Source: UniProtKB
    5. double-stranded DNA binding Source: UniProtKB
    6. single-stranded DNA binding Source: UniProtKB
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. base-excision repair Source: UniProtKB
    2. DNA catabolic process, endonucleolytic Source: GOC
    3. nucleotide-excision repair Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endonuclease 8-like 3 (EC:3.2.2.-, EC:4.2.99.18)
    Alternative name(s):
    DNA glycosylase FPG2
    DNA glycosylase/AP lyase Neil3
    Endonuclease VIII-like 3
    Nei-like protein 3
    Gene namesi
    Name:NEIL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:24573. NEIL3.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21V → P: No effect on AP lyase activity. Impairs monofunctional glycosylase activity. 2 Publications
    Mutagenesisi3 – 31E → A: No effect on AP lyase activity. 1 Publication
    Mutagenesisi81 – 811K → A: Loss of glycosylase and lyase activities. 1 Publication
    Mutagenesisi276 – 2761C → S: Abolishes AP lyase activity. 1 Publication
    Mutagenesisi279 – 2791C → S: Abolishes AP lyase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134889634.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedCurated
    Chaini2 – 605604Endonuclease 8-like 3PRO_0000170910Add
    BLAST

    Proteomic databases

    MaxQBiQ8TAT5.
    PaxDbiQ8TAT5.
    PRIDEiQ8TAT5.

    PTM databases

    PhosphoSiteiQ8TAT5.

    Expressioni

    Tissue specificityi

    Expressed in keratinocytes and embryonic fibroblasts (at protein level). Also detected in thymus, testis and fetal lung primary fibroblasts.4 Publications

    Developmental stagei

    Up-regulated during early S phase of the cell cycle, and sustained through G/M phase. Low expression levels in quiescent cells.1 Publication

    Gene expression databases

    ArrayExpressiQ8TAT5.
    BgeeiQ8TAT5.
    CleanExiHS_NEIL3.
    GenevestigatoriQ8TAT5.

    Interactioni

    Protein-protein interaction databases

    BioGridi120538. 2 interactions.
    STRINGi9606.ENSP00000264596.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TAT5.
    SMRiQ8TAT5. Positions 2-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The N-terminal region (2-281) contains the glycosylase and lyase activities.By similarity

    Sequence similaritiesi

    Belongs to the FPG family.PROSITE-ProRule annotation
    Contains 1 FPG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri247 – 28135FPG-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri317 – 34630RanBP2-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0266.
    HOGENOMiHOG000113754.
    HOVERGENiHBG052594.
    InParanoidiQ8TAT5.
    KOiK10569.
    OMAiICFFDSS.
    OrthoDBiEOG7W153D.
    PhylomeDBiQ8TAT5.
    TreeFamiTF331502.

    Family and domain databases

    InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
    IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
    IPR012319. DNA_glycosylase/AP_lyase_cat.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR000214. Znf_DNA_glyclase/AP_lyase.
    IPR010666. Znf_GRF.
    IPR001876. Znf_RanBP2.
    [Graphical view]
    PfamiPF06831. H2TH. 1 hit.
    PF06839. zf-GRF. 2 hits.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view]
    SMARTiSM00547. ZnF_RBZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46946. SSF46946. 1 hit.
    SSF81624. SSF81624. 1 hit.
    PROSITEiPS51068. FPG_CAT. 1 hit.
    PS01242. ZF_FPG_1. 1 hit.
    PS51066. ZF_FPG_2. 1 hit.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8TAT5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVEGPGCTLN GEKIRARVLP GQAVTGVRGS ALRSLQGRAL RLAASTVVVS    50
    PQAAALNNDS SQNVLSLFNG YVYSGVETLG KELFMYFGPK ALRIHFGMKG 100
    FIMINPLEYK YKNGASPVLE VQLTKDLICF FDSSVELRNS MESQQRIRMM 150
    KELDVCSPEF SFLRAESEVK KQKGRMLGDV LMDQNVLPGV GNIIKNEALF 200
    DSGLHPAVKV CQLTDEQIHH LMKMIRDFSI LFYRCRKAGL ALSKHYKVYK 250
    RPNCGQCHCR ITVCRFGDNN RMTYFCPHCQ KENPQHVDIC KLPTRNTIIS 300
    WTSSRVDHVM DSVARKSEEH WTCVVCTLIN KPSSKACDAC LTSRPIDSVL 350
    KSEENSTVFS HLMKYPCNTF GKPHTEVKIN RKTAFGTTTL VLTDFSNKSS 400
    TLERKTKQNQ ILDEEFQNSP PASVCLNDIQ HPSKKTTNDI TQPSSKVNIS 450
    PTISSESKLF SPAHKKPKTA QYSSPELKSC NPGYSNSELQ INMTDGPRTL 500
    NPDSPRCSKH NRLCILRVVG KDGENKGRQF YACPLPREAQ CGFFEWADLS 550
    FPFCNHGKRS TMKTVLKIGP NNGKNFFVCP LGKEKQCNFF QWAENGPGIK 600
    IIPGC 605
    Length:605
    Mass (Da):67,769
    Last modified:August 10, 2010 - v3
    Checksum:i528B17873ABC9D89
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351L → P in BAA91860. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381R → C.1 Publication
    Corresponds to variant rs34007209 [ dbSNP | Ensembl ].
    VAR_025806
    Natural varianti58 – 581N → NN.1 Publication
    VAR_025807
    Natural varianti76 – 761V → M.1 Publication
    Corresponds to variant rs34112288 [ dbSNP | Ensembl ].
    VAR_025808
    Natural varianti117 – 1171P → R.2 Publications
    Corresponds to variant rs7689099 [ dbSNP | Ensembl ].
    VAR_020590
    Natural varianti172 – 1721Q → H.1 Publication
    Corresponds to variant rs17064658 [ dbSNP | Ensembl ].
    VAR_025809
    Natural varianti286 – 2861H → R.1 Publication
    Corresponds to variant rs34193982 [ dbSNP | Ensembl ].
    VAR_025810
    Natural varianti346 – 3461I → V.1 Publication
    Corresponds to variant rs17064676 [ dbSNP | Ensembl ].
    VAR_025811
    Natural varianti443 – 4431P → L.4 Publications
    Corresponds to variant rs13112358 [ dbSNP | Ensembl ].
    VAR_020591
    Natural varianti471 – 4711Q → H.4 Publications
    Corresponds to variant rs13112390 [ dbSNP | Ensembl ].
    VAR_025812
    Natural varianti520 – 5201G → R.4 Publications
    Corresponds to variant rs1876268 [ dbSNP | Ensembl ].
    VAR_020592
    Natural varianti547 – 5471A → S.1 Publication
    Corresponds to variant rs36005630 [ dbSNP | Ensembl ].
    VAR_025813
    Natural varianti556 – 5561H → R.1 Publication
    Corresponds to variant rs35418725 [ dbSNP | Ensembl ].
    VAR_025814

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079071 mRNA. Translation: BAC06479.1.
    AK001720 mRNA. Translation: BAA91860.1.
    DQ310721 Genomic DNA. Translation: ABC40719.1.
    AC027627 Genomic DNA. No translation available.
    BC025954 mRNA. Translation: AAH25954.1.
    CCDSiCCDS3828.1.
    RefSeqiNP_060718.2. NM_018248.2.
    UniGeneiHs.405467.

    Genome annotation databases

    EnsembliENST00000264596; ENSP00000264596; ENSG00000109674.
    GeneIDi55247.
    KEGGihsa:55247.
    UCSCiuc003iut.2. human.

    Polymorphism databases

    DMDMi302393810.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079071 mRNA. Translation: BAC06479.1 .
    AK001720 mRNA. Translation: BAA91860.1 .
    DQ310721 Genomic DNA. Translation: ABC40719.1 .
    AC027627 Genomic DNA. No translation available.
    BC025954 mRNA. Translation: AAH25954.1 .
    CCDSi CCDS3828.1.
    RefSeqi NP_060718.2. NM_018248.2.
    UniGenei Hs.405467.

    3D structure databases

    ProteinModelPortali Q8TAT5.
    SMRi Q8TAT5. Positions 2-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120538. 2 interactions.
    STRINGi 9606.ENSP00000264596.

    PTM databases

    PhosphoSitei Q8TAT5.

    Polymorphism databases

    DMDMi 302393810.

    Proteomic databases

    MaxQBi Q8TAT5.
    PaxDbi Q8TAT5.
    PRIDEi Q8TAT5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264596 ; ENSP00000264596 ; ENSG00000109674 .
    GeneIDi 55247.
    KEGGi hsa:55247.
    UCSCi uc003iut.2. human.

    Organism-specific databases

    CTDi 55247.
    GeneCardsi GC04P178230.
    HGNCi HGNC:24573. NEIL3.
    MIMi 608934. gene.
    neXtProti NX_Q8TAT5.
    PharmGKBi PA134889634.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0266.
    HOGENOMi HOG000113754.
    HOVERGENi HBG052594.
    InParanoidi Q8TAT5.
    KOi K10569.
    OMAi ICFFDSS.
    OrthoDBi EOG7W153D.
    PhylomeDBi Q8TAT5.
    TreeFami TF331502.

    Miscellaneous databases

    GeneWikii NEIL3_(gene).
    GenomeRNAii 55247.
    NextBioi 59296.
    PROi Q8TAT5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TAT5.
    Bgeei Q8TAT5.
    CleanExi HS_NEIL3.
    Genevestigatori Q8TAT5.

    Family and domain databases

    InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
    IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
    IPR012319. DNA_glycosylase/AP_lyase_cat.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR000214. Znf_DNA_glyclase/AP_lyase.
    IPR010666. Znf_GRF.
    IPR001876. Znf_RanBP2.
    [Graphical view ]
    Pfami PF06831. H2TH. 1 hit.
    PF06839. zf-GRF. 2 hits.
    PF00641. zf-RanBP. 1 hit.
    [Graphical view ]
    SMARTi SM00547. ZnF_RBZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46946. SSF46946. 1 hit.
    SSF81624. SSF81624. 1 hit.
    PROSITEi PS51068. FPG_CAT. 1 hit.
    PS01242. ZF_FPG_1. 1 hit.
    PS51066. ZF_FPG_2. 1 hit.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 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], VARIANTS LEU-443; HIS-471 AND ARG-520.
      Tissue: Skin.
    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], VARIANTS LEU-443; HIS-471 AND ARG-520.
    3. NIEHS SNPs program
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-38; ASN-58 INS; MET-76; ARG-117; HIS-172; ARG-286; VAL-346; LEU-443; HIS-471; ARG-520; SER-547 AND ARG-556.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANTS ARG-117; LEU-443; HIS-471 AND ARG-520.
      Tissue: B-cell.
    6. "Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA."
      Morland I., Rolseth V., Luna L., Rognes T., Bjoeraas M., Seeberg E.
      Nucleic Acids Res. 30:4926-4936(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "Hematopoietic tissue-specific expression of mouse Neil3 for endonuclease VIII-like protein."
      Torisu K., Tsuchimoto D., Ohnishi Y., Nakabeppu Y.
      J. Biochem. 138:763-772(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "Expression patterns of Neil3 during embryonic brain development and neoplasia."
      Hildrestrand G.A., Neurauter C.G., Diep D.B., Castellanos C.G., Krauss S., Bjoras M., Luna L.
      BMC Neurosci. 10:45-45(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Human Nei-like protein NEIL3 has AP lyase activity specific for single-stranded DNA and confers oxidative stress resistance in Escherichia coli mutant."
      Takao M., Oohata Y., Kitadokoro K., Kobayashi K., Iwai S., Yasui A., Yonei S., Zhang Q.M.
      Genes Cells 14:261-270(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF VAL-2; GLU-3; CYS-276 AND CYS-279.
    10. "Expression and purification of NEIL3, a human DNA glycosylase homolog."
      Krokeide S.Z., Bolstad N., Laerdahl J.K., Bjoras M., Luna L.
      Protein Expr. Purif. 65:160-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Release from quiescence stimulates the expression of human NEIL3 under the control of the Ras dependent ERK-MAP kinase pathway."
      Neurauter C.G., Luna L., Bjoras M.
      DNA Repair 11:401-409(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    12. "Expression and purification of active mouse and human NEIL3 proteins."
      Liu M., Bandaru V., Holmes A., Averill A.M., Cannan W., Wallace S.S.
      Protein Expr. Purif. 84:130-139(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A GLYCOSYLASE, PROBABLE CLEAVAGE OF INITIATOR METHIONINE.
    13. "Human NEIL3 is mainly a monofunctional DNA glycosylase removing spiroimindiohydantoin and guanidinohydantoin."
      Krokeide S.Z., Laerdahl J.K., Salah M., Luna L., Cederkvist F.H., Fleming A.M., Burrows C.J., Dalhus B., Bjoras M.
      DNA Repair 12:1159-1164(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, PROBABLE CLEAVAGE OF INITIATOR METHIONINE, MUTAGENESIS OF VAL-2 AND LYS-81.

    Entry informationi

    Entry nameiNEIL3_HUMAN
    AccessioniPrimary (citable) accession number: Q8TAT5
    Secondary accession number(s): Q2PPJ3, Q8NG51, Q9NV95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: August 10, 2010
    Last modified: October 1, 2014
    This is version 105 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

    Caution

    Was originally thought to be inactive as a glycosylase (PMID:12200441,PMID:19121397), but recent reports (PMID:22569481, PMID:20185759) demonstrate that cleavage of the initiator methionine is essential for catalytic activity.Curated

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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