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Q969S2

- NEIL2_HUMAN

UniProt

Q969S2 - NEIL2_HUMAN

Protein

Endonuclease 8-like 2

Gene

NEIL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 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.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

    Enzyme regulationi

    Acetylation of Lys-50 leads to loss of DNA nicking activity. Acetylation of Lys-154 has no effect.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21Schiff-base intermediate with DNACurated
    Active sitei3 – 31Proton donorCurated
    Active sitei50 – 501Proton donor; for beta-elimination activityCurated
    Binding sitei231 – 2311DNABy similarity
    Active sitei310 – 3101Proton donor; for delta-elimination activityCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri284 – 32037FPG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. damaged DNA binding Source: InterPro
    2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
    3. hydrolase activity, hydrolyzing N-glycosyl compounds Source: InterPro
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. base-excision repair Source: InterPro
    2. 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 2 (EC:3.2.2.-, EC:4.2.99.18)
    Alternative name(s):
    DNA glycosylase/AP lyase Neil2
    DNA-(apurinic or apyrimidinic site) lyase Neil2
    Endonuclease VIII-like 2
    Nei homolog 2
    Short name:
    NEH2
    Nei-like protein 2
    Gene namesi
    Name:NEIL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:18956. NEIL2.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleus Source: UniProtKB-SubCell
    3. spindle microtubule Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501K → R: Loss of glycosylase and AP lyase activity. 2 Publications
    Mutagenesisi154 – 1541K → R: No effect on glycosylase and AP lyase activity. 1 Publication
    Mutagenesisi291 – 2911C → S: Loss of glycosylase and AP lyase activity. 1 Publication
    Mutagenesisi295 – 2951H → A: Loss of glycosylase and AP lyase activity. 1 Publication
    Mutagenesisi310 – 3101R → Q: Strongly reduces strand AP lyase activity. 1 Publication
    Mutagenesisi315 – 3151C → S: Loss of glycosylase and AP lyase activity. 1 Publication
    Mutagenesisi318 – 3181C → S: Loss of glycosylase and AP lyase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA38769.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 332331Endonuclease 8-like 2PRO_0000170908Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501N6-acetyllysine1 Publication
    Modified residuei154 – 1541N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ969S2.
    PaxDbiQ969S2.
    PRIDEiQ969S2.

    PTM databases

    PhosphoSiteiQ969S2.

    Expressioni

    Tissue specificityi

    Detected in testis, skeletal muscle, heart, brain, placenta, lung, pancreas, kidney and liver.1 Publication

    Gene expression databases

    ArrayExpressiQ969S2.
    BgeeiQ969S2.
    CleanExiHS_NEIL2.
    GenevestigatoriQ969S2.

    Interactioni

    Subunit structurei

    Binds EP300.

    Protein-protein interaction databases

    BioGridi128946. 4 interactions.
    MINTiMINT-4720021.
    STRINGi9606.ENSP00000284503.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VZPmodel-A192-319[»]
    ProteinModelPortaliQ969S2.
    SMRiQ969S2. Positions 129-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The zinc-finger domain is important for DNA binding.

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri284 – 32037FPG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG73546.
    HOGENOMiHOG000069913.
    HOVERGENiHBG082014.
    InParanoidiQ969S2.
    KOiK10568.
    OMAiSVRKFHH.
    OrthoDBiEOG7Z69CR.
    PhylomeDBiQ969S2.
    TreeFamiTF331502.

    Family and domain databases

    InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
    IPR012319. DNA_glycosylase/AP_lyase_cat.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR000214. Znf_DNA_glyclase/AP_lyase.
    [Graphical view]
    PfamiPF01149. Fapy_DNA_glyco. 1 hit.
    PF06831. H2TH. 1 hit.
    [Graphical view]
    SUPFAMiSSF46946. SSF46946. 1 hit.
    PROSITEiPS51068. FPG_CAT. 1 hit.
    PS51066. ZF_FPG_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q969S2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPEGPLVRKF HHLVSPFVGQ QVVKTGGSSK KLQPASLQSL WLQDTQVHGK    50
    KLFLRFDLDE EMGPPGSSPT PEPPQKEVQK EGAADPKQVG EPSGQKTLDG 100
    SSRSAELVPQ GEDDSEYLER DAPAGDAGRW LRVSFGLFGS VWVNDFSRAK 150
    KANKRGDWRD PSPRLVLHFG GGGFLAFYNC QLSWSSSPVV TPTCDILSEK 200
    FHRGQALEAL GQAQPVCYTL LDQRYFSGLG NIIKNEALYR AGIHPLSLGS 250
    VLSASRREVL VDHVVEFSTA WLQGKFQGRP QHTQVYQKEQ CPAGHQVMKE 300
    AFGPEDGLQR LTWWCPQCQP QLSEEPEQCQ FS 332
    Length:332
    Mass (Da):36,826
    Last modified:January 23, 2007 - v3
    Checksum:i8A8E76B75ABADE6D
    GO
    Isoform 2 (identifier: Q969S2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         79-94: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:316
    Mass (Da):35,247
    Checksum:i3183DDC0C41936DC
    GO
    Isoform 3 (identifier: Q969S2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:271
    Mass (Da):29,930
    Checksum:iA23E2B89F5256AE6
    GO
    Isoform 4 (identifier: Q969S2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         48-163: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:216
    Mass (Da):24,136
    Checksum:i250E84C5B5DAF3CB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti70 – 701T → S.1 Publication
    Corresponds to variant rs8191611 [ dbSNP | Ensembl ].
    VAR_020585
    Natural varianti103 – 1031R → Q.2 Publications
    Corresponds to variant rs8191613 [ dbSNP | Ensembl ].
    VAR_020586
    Natural varianti103 – 1031R → W.1 Publication
    Corresponds to variant rs8191612 [ dbSNP | Ensembl ].
    VAR_020587
    Natural varianti257 – 2571R → L.1 Publication
    Corresponds to variant rs8191664 [ dbSNP | Ensembl ].
    VAR_020588
    Natural varianti304 – 3041P → T.1 Publication
    Corresponds to variant rs8191666 [ dbSNP | Ensembl ].
    VAR_020589

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6161Missing in isoform 3. 1 PublicationVSP_012208Add
    BLAST
    Alternative sequencei48 – 163116Missing in isoform 4. 1 PublicationVSP_043343Add
    BLAST
    Alternative sequencei79 – 9416Missing in isoform 2. 1 PublicationVSP_012209Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079070 mRNA. Translation: BAC06478.1.
    AK056206 mRNA. Translation: BAB71120.1.
    AK097389 mRNA. Translation: BAC05030.1.
    AK294224 mRNA. Translation: BAG57528.1.
    BX537529 mRNA. Translation: CAD97774.1.
    AY306127 Genomic DNA. Translation: AAP45052.1.
    AC069185 Genomic DNA. No translation available.
    BC013952 mRNA. Translation: AAH13952.1.
    BC013964 mRNA. Translation: AAH13964.1.
    CCDSiCCDS47802.1. [Q969S2-4]
    CCDS47803.1. [Q969S2-3]
    CCDS5984.1. [Q969S2-1]
    RefSeqiNP_001129218.1. NM_001135746.1. [Q969S2-1]
    NP_001129219.1. NM_001135747.1. [Q969S2-3]
    NP_001129220.1. NM_001135748.1. [Q969S2-4]
    NP_659480.1. NM_145043.2. [Q969S2-1]
    XP_005272438.1. XM_005272381.1. [Q969S2-1]
    XP_005272439.1. XM_005272382.1. [Q969S2-3]
    XP_005272440.1. XM_005272383.1. [Q969S2-3]
    UniGeneiHs.293818.

    Genome annotation databases

    EnsembliENST00000284503; ENSP00000284503; ENSG00000154328. [Q969S2-1]
    ENST00000403422; ENSP00000384070; ENSG00000154328. [Q969S2-3]
    ENST00000436750; ENSP00000394023; ENSG00000154328. [Q969S2-1]
    ENST00000455213; ENSP00000397538; ENSG00000154328. [Q969S2-1]
    ENST00000528323; ENSP00000435657; ENSG00000154328. [Q969S2-4]
    GeneIDi252969.
    KEGGihsa:252969.
    UCSCiuc003wue.2. human. [Q969S2-1]
    uc011kxd.1. human. [Q969S2-4]

    Polymorphism databases

    DMDMi56404653.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079070 mRNA. Translation: BAC06478.1 .
    AK056206 mRNA. Translation: BAB71120.1 .
    AK097389 mRNA. Translation: BAC05030.1 .
    AK294224 mRNA. Translation: BAG57528.1 .
    BX537529 mRNA. Translation: CAD97774.1 .
    AY306127 Genomic DNA. Translation: AAP45052.1 .
    AC069185 Genomic DNA. No translation available.
    BC013952 mRNA. Translation: AAH13952.1 .
    BC013964 mRNA. Translation: AAH13964.1 .
    CCDSi CCDS47802.1. [Q969S2-4 ]
    CCDS47803.1. [Q969S2-3 ]
    CCDS5984.1. [Q969S2-1 ]
    RefSeqi NP_001129218.1. NM_001135746.1. [Q969S2-1 ]
    NP_001129219.1. NM_001135747.1. [Q969S2-3 ]
    NP_001129220.1. NM_001135748.1. [Q969S2-4 ]
    NP_659480.1. NM_145043.2. [Q969S2-1 ]
    XP_005272438.1. XM_005272381.1. [Q969S2-1 ]
    XP_005272439.1. XM_005272382.1. [Q969S2-3 ]
    XP_005272440.1. XM_005272383.1. [Q969S2-3 ]
    UniGenei Hs.293818.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VZP model - A 192-319 [» ]
    ProteinModelPortali Q969S2.
    SMRi Q969S2. Positions 129-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128946. 4 interactions.
    MINTi MINT-4720021.
    STRINGi 9606.ENSP00000284503.

    PTM databases

    PhosphoSitei Q969S2.

    Polymorphism databases

    DMDMi 56404653.

    Proteomic databases

    MaxQBi Q969S2.
    PaxDbi Q969S2.
    PRIDEi Q969S2.

    Protocols and materials databases

    DNASUi 252969.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284503 ; ENSP00000284503 ; ENSG00000154328 . [Q969S2-1 ]
    ENST00000403422 ; ENSP00000384070 ; ENSG00000154328 . [Q969S2-3 ]
    ENST00000436750 ; ENSP00000394023 ; ENSG00000154328 . [Q969S2-1 ]
    ENST00000455213 ; ENSP00000397538 ; ENSG00000154328 . [Q969S2-1 ]
    ENST00000528323 ; ENSP00000435657 ; ENSG00000154328 . [Q969S2-4 ]
    GeneIDi 252969.
    KEGGi hsa:252969.
    UCSCi uc003wue.2. human. [Q969S2-1 ]
    uc011kxd.1. human. [Q969S2-4 ]

    Organism-specific databases

    CTDi 252969.
    GeneCardsi GC08P011627.
    HGNCi HGNC:18956. NEIL2.
    MIMi 608933. gene.
    neXtProti NX_Q969S2.
    PharmGKBi PA38769.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG73546.
    HOGENOMi HOG000069913.
    HOVERGENi HBG082014.
    InParanoidi Q969S2.
    KOi K10568.
    OMAi SVRKFHH.
    OrthoDBi EOG7Z69CR.
    PhylomeDBi Q969S2.
    TreeFami TF331502.

    Miscellaneous databases

    ChiTaRSi NEIL2. human.
    GeneWikii NEIL2.
    GenomeRNAii 252969.
    NextBioi 92030.
    PROi Q969S2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q969S2.
    Bgeei Q969S2.
    CleanExi HS_NEIL2.
    Genevestigatori Q969S2.

    Family and domain databases

    InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
    IPR012319. DNA_glycosylase/AP_lyase_cat.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR000214. Znf_DNA_glyclase/AP_lyase.
    [Graphical view ]
    Pfami PF01149. Fapy_DNA_glyco. 1 hit.
    PF06831. H2TH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46946. SSF46946. 1 hit.
    PROSITEi PS51068. FPG_CAT. 1 hit.
    PS51066. ZF_FPG_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] (ISOFORM 1), VARIANT GLN-103.
    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] (ISOFORMS 1; 3 AND 4).
      Tissue: Amygdala and Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Fetal kidney.
    4. NIEHS SNPs program
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-70; GLN-103; TRP-103; LEU-257 AND THR-304.
    5. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Muscle.
    7. "Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions."
      Hazra T.K., Kow Y.W., Hatahet Z., Imhoff B., Boldogh I., Mokkapati S.K., Mitra S., Izumi T.
      J. Biol. Chem. 277:30417-30420(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "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-50.
    9. "Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity."
      Bhakat K.K., Hazra T.K., Mitra S.
      Nucleic Acids Res. 32:3033-3039(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 40-57 AND 142-161, FUNCTION, MUTAGENESIS OF LYS-50 AND LYS-154, INTERACTION WITH EP300, ACETYLATION AT LYS-50 AND LYS-154.
    10. "Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein."
      Das A., Rajagopalan L., Mathura V.S., Rigby S.J., Mitra S., Hazra T.K.
      J. Biol. Chem. 279:47132-47138(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-291; HIS-295; ARG-310; CYS-315 AND CYS-318, FUNCTION, IDENTIFICATION OF ZINC-FINGER, ZINC-BINDING, 3D-STRUCTURE MODELING OF 192-319, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiNEIL2_HUMAN
    AccessioniPrimary (citable) accession number: Q969S2
    Secondary accession number(s): B4DFR7
    , Q7Z3Q7, Q8N842, Q8NG52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 112 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, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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