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NEIL1 (nei endonuclease VIII-like 1 (E. coli))

Written2007-07Masaya Suzuki, Kazuya Shinmura, Haruhiko Sugimura
Department of Pathology, Hamamatsu University School of Medicine, 1-20-1, Handayama, Hamamatsu, Shizuoka 431-3192, Japan

(Note : for Links provided by Atlas : click)


Alias (NCBI)FLJ22402
HGNC Alias symbFLJ22402
HGNC Alias nameDNA endonuclease eight-like glycosylase 1
HGNC Previous namenei endonuclease VIII-like 1 (E. coli)
LocusID (NCBI) 79661
Atlas_Id 41519
Location 15q24.2  [Link to chromosome band 15q24]
Location_base_pair Starts at 75347039 and ends at 75357115 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping NEIL1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
NEIL1 (15q24.2)::NEIL1 (15q24.2)


Description The NEIL1 gene maps on chromosome 15q24.2 spanning 8,179bp. It contains 11 exons, and the orientation is plus strand.
Transcription The transcript of 1,828bp, expressed in Brain, Liver, Lung, Kidney, Colon, and Stomach. The NEIL1 gene is up-regulated during S-phase.


Description NEIL1 encodes 390 amino acids, theoretical molecular weight is 43684 Da, Formamidopyrimidine-DNA glycosylase N-terminal domain and Formamidopyrimidine-DNA glycosylase H2TH domain.
Localisation Nucleus, centrosome, and mitotic condensed chromosomes.
Function (1) Bifunctional DNA glycosylase and apurinic/apyrimidinic (AP) lyase that catalyzes beta- and delta-elimination reactions at the site of damaged base.
(2) Reported substrates: thymine glycol (Tg), 5-hydroxycytosine, 5-hydroxyuracil, 5,6-dihydrouracil, 5,6-dihydrothymine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG), 4,6-diamino-5-formamidopyrimidine (FapyA), 5-formyluracil, 5-hydroxymethyluracil, spiroiminodihydantoin (Sp), guanidinohydantoin, (Gh) and 8-hydroxyguanine.
(3) Since NEIL1 catalyzes beta- and delta-elimination reactions, the protein generates DNA strand breaks with 3' phosphate termini. In mammalian cells, this 3' phosphate is removed by polynucleotide kinase, but not by . NEIL1 stably interacts with other BER proteins, DNA polymerase beta and DNA ligase III alpha.
(4) In mammalian BER, DNA glycosylases generate abasic (AP) sites, which are then converted to deoxyribo-5'-phosphate (dRP) and excised by a dRP lyase (dRPase) activity of DNA polymerase beta. Since NEIL1 also has dRPase activity, NEIL1 has a role as a backup dRPase in mammalian cells.
(5) NEIL1 has a repair activity for oxidized bases in single-strand DNA and bubble DNA, suggesting a possibility that NEIL1 is preferentially involved in repair of lesions in DNA bubbles generated during transcription and/or replication.
(6) Proteins that associate and stimulate the repair activity of NEIL1: a) The (WRN), a member of RecQ family of DNA helicases, b) , , and as individual proteins and as the 9-1-1 complex.
(7) The major DNA glycosylase for the excision of 8-hydroxyguanine is . In the repair of 8-ydroxyguanine by OGG1, after excising the base lesion, OGG1 remains bound to the resulting AP site and does not turn over efficiently. The APE1, which cleaves the phosphodiester bond 5' to the AP site, displaces the bound OGG1 and thus increases its turnover. NEIL1 stimulates turnover of OGG1 in a fashion similar to that of APE1, and carries out beta/delta- elimination at the AP site.
(8) Although OGG1 has limited activity on 8-hydroxyguanine lesion located in the vicinity of the 3' end of a DNA single-strand break, NEIL1 effectively excises the 3' end proximal 8-hydroxyguanine lesion. NEIL1 also effectively excises 5-hydroxyuracil lesions located in the proximity of the 3'-end of a DNA single-strand break. (9) The NEIL1 gene is induced by reactive oxygen species.
Homology Homo sapiens: (NP_659480, 20.1%), (NP_060718, 15.0%) using the CLUSTALW software.

Implicated in

Entity Gastric cancer
Note The following is the abstract of the paper by Shinmura K. et al. (Carcinogenesis, 2004). Oxidized DNA base lesions, such as thymine glycol (Tg) and 8-hydroxyguanine, are often toxic and mutagenic and have been implicated in carcinogenesis. To clarify whether NEIL1 protein, which exhibits excision repair activity towards such base lesions, is involved in gastric carcinogenesis, we examined 71 primary gastric cancers from Japanese patients and four gastric cancer cell lines for mutations and genetic polymorphisms of the NEIL1 gene. We also examined 20 blood samples from Chinese patients for NEIL1 genetic polymorphisms. Three mutations (c.82_84delGAG:p.Glu28del, c.936G > A and c.1000A > G:p.Arg334Gly) and two genetic polymorphisms were identified. When the excision repair activity towards double-stranded oligonucleotide containing a Tg:A base pair was compared among six types of recombinant NEIL1 proteins, p.Glu28del-type NEIL1, found in a primary case, was found to exhibit an extremely low activity level. Moreover, c.936G > A, located in the last nucleotide of exon 10 and detected in the KATO-III cell line, was shown to be associated with a splicing abnormality using an in vivo splicing assay. An immunofluorescence analysis showed that the wild-type NEIL1 protein, but not the truncated protein encoded by the abnormal transcript arising from the c.936G > A mutation, was localized in the nucleus, suggesting that the truncated protein is unlikely to be capable of repairing nuclear DNA. An expression analysis revealed that NEIL1 mRNA expression was reduced in six of 13 (46%) primary gastric cancer specimens that were examined. These results suggest that low NEIL1 activities arising from mutations and reduced expression may be involved in the pathogenesis in a subset of gastric cancers.


Different organization of base excision repair of uracil in DNA in nuclei and mitochondria and selective upregulation of mitochondrial uracil-DNA glycosylase after oxidative stress.
Akbari M, Otterlei M, Peña-Diaz J, Krokan HE
Neuroscience. 2007 ; 145 (4) : 1201-1212.
PMID 17101234
Action of human endonucleases III and VIII upon DNA-containing tandem dihydrouracil.
Ali MM, Hazra TK, Hong D, Kow YW
DNA repair. 2005 ; 4 (6) : 679-686.
PMID 15907775
Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA-repair enzyme that recognizes oxidative DNA damage.
Bandaru V, Cooper W, Wallace SS, Doublié S
Acta crystallographica. Section D, Biological crystallography. 2004 ; 60 (Pt 6) : 1142-1144.
PMID 15159582
A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII.
Bandaru V, Sunkara S, Wallace SS, Bond JP
DNA repair. 2002 ; 1 (7) : 517-529.
PMID 12509226
Human endonuclease VIII-like (NEIL) proteins in the giant DNA Mimivirus.
Bandaru V, Zhao X, Newton MR, Burrows CJ, Wallace SS
DNA repair. 2007 ; 6 (11) : 1629-1641.
PMID 17627905
The human Werner syndrome protein stimulates repair of oxidative DNA base damage by the DNA glycosylase NEIL1.
Das A, Boldogh I, Lee JW, Harrigan JA, Hegde ML, Piotrowski J, de Souza Pinto N, Ramos W, Greenberg MM, Hazra TK, Mitra S, Bohr VA
The Journal of biological chemistry. 2007 ; 282 (36) : 26591-26602.
PMID 17611195
Induction of the human oxidized base-specific DNA glycosylase NEIL1 by reactive oxygen species.
Das A, Hazra TK, Boldogh I, Mitra S, Bhakat KK
The Journal of biological chemistry. 2005 ; 280 (42) : 35272-35280.
PMID 16118226
Major oxidative products of cytosine are substrates for the nucleotide incision repair pathway.
Daviet S, Couvé-Privat S, Gros L, Shinozuka K, Ide H, Saparbaev M, Ishchenko AA
DNA repair. 2007 ; 6 (1) : 8-18.
PMID 16978929
Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2.
Dou H, Mitra S, Hazra TK
The Journal of biological chemistry. 2003 ; 278 (50) : 49679-49684.
PMID 14522990
The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity.
Doublié S, Bandaru V, Bond JP, Wallace SS
Proceedings of the National Academy of Sciences of the United States of America. 2004 ; 101 (28) : 10284-10289.
PMID 15232006
Deoxyribophosphate lyase activity of mammalian endonuclease VIII-like proteins.
Grin IR, Khodyreva SN, Nevinsky GA, Zharkov DO
FEBS letters. 2006 ; 580 (20) : 4916-4922.
PMID 16920106
The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates NEIL1 glycosylase.
Guan X, Bai H, Shi G, Theriot CA, Hazra TK, Mitra S, Lu AL
Nucleic acids research. 2007 ; 35 (8) : 2463-2472.
PMID 17395641
Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2.
Hailer MK, Slade PG, Martin BD, Rosenquist TA, Sugden KD
DNA repair. 2005 ; 4 (1) : 41-50.
PMID 15533836
Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA.
Hazra TK, Izumi T, Boldogh I, Imhoff B, Kow YW, Jaruga P, Dizdaroglu M, Mitra S
Proceedings of the National Academy of Sciences of the United States of America. 2002 ; 99 (6) : 3523-3528.
PMID 11904416
Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions.
Hazra TK, Kow YW, Hatahet Z, Imhoff B, Boldogh I, Mokkapati SK, Mitra S, Izumi T
The Journal of biological chemistry. 2002 ; 277 (34) : 30417-30420.
PMID 12097317
Purification and characterization of NEIL1 and NEIL2, members of a distinct family of mammalian DNA glycosylases for repair of oxidized bases.
Hazra TK, Mitra S
Methods in enzymology. 2006 ; 408 : 33-48.
PMID 16793361
Human NEIL1 localizes with the centrosomes and condensed chromosomes during mitosis.
Hildrestrand GA, Rolseth V, Bj&oring;rå M, Luna L
DNA repair. 2007 ; 6 (10) : 1425-1433.
PMID 17556049
Repair of formamidopyrimidines in DNA involves different glycosylases: role of the OGG1, NTH1, and NEIL1 enzymes.
Hu J, de Souza-Pinto NC, Haraguchi K, Hogue BA, Jaruga P, Greenberg MM, Dizdaroglu M, Bohr VA
The Journal of biological chemistry. 2005 ; 280 (49) : 40544-40551.
PMID 16221681
Expression of the oxidative base excision repair enzymes is not induced in TK6 human lymphoblastoid cells after low doses of ionizing radiation.
Inoue M, Shen GP, Chaudhry MA, Galick H, Blaisdell JO, Wallace SS
Radiation research. 2004 ; 161 (4) : 409-417.
PMID 15038771
Mouse NEIL1 protein is specific for excision of 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine from oxidatively damaged DNA.
Jaruga P, Birincioglu M, Rosenquist TA, Dizdaroglu M
Biochemistry. 2004 ; 43 (50) : 15909-15914.
PMID 15595846
Lesion specificity in the base excision repair enzyme hNeil1: modeling and dynamics studies.
Jia L, Shafirovich V, Geacintov NE, Broyde S
Biochemistry. 2007 ; 46 (18) : 5305-5314.
PMID 17432829
Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions.
Katafuchi A, Nakano T, Masaoka A, Terato H, Iwai S, Hanaoka F, Ide H
The Journal of biological chemistry. 2004 ; 279 (14) : 14464-14471.
PMID 14734554
Cross-linking of 2-deoxyribonolactone and its beta-elimination product by base excision repair enzymes.
Kroeger KM, Hashimoto M, Kow YW, Greenberg MM
Biochemistry. 2003 ; 42 (8) : 2449-2455.
PMID 12600212
Stereoselective excision of thymine glycol from oxidatively damaged DNA.
Miller H, Fernandes AS, Zaika E, McTigue MM, Torres MC, Wente M, Iden CR, Grollman AP
Nucleic acids research. 2004 ; 32 (1) : 338-345.
PMID 14726482
Stimulation of DNA glycosylase activity of OGG1 by NEIL1: functional collaboration between two human DNA glycosylases.
Mokkapati SK, Wiederhold L, Hazra TK, Mitra S
Biochemistry. 2004 ; 43 (36) : 11596-11604.
PMID 15350146
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, Bj&oring;rås M, Seeberg E
Nucleic acids research. 2002 ; 30 (22) : 4926-4936.
PMID 12433996
Repair of thymine glycol by hNth1 and hNeil1 is modulated by base pairing and cis-trans epimerization.
Ocampo-Hafalla MT, Altamirano A, Basu AK, Chan MK, Ocampo JE, Cummings A Jr, Boorstein RJ, Cunningham RP, Teebor GW
DNA repair. 2006 ; 5 (4) : 444-454.
PMID 16446124
NEIL1 is the major DNA glycosylase that processes 5-hydroxyuracil in the proximity of a DNA single-strand break.
Parsons JL, Kavli B, Slupphaug G, Dianov GL
Biochemistry. 2007 ; 46 (13) : 4158-4163.
PMID 17348689
The novel DNA glycosylase, NEIL1, protects mammalian cells from radiation-mediated cell death.
Rosenquist TA, Zaika E, Fernandes AS, Zharkov DO, Miller H, Grollman AP
DNA repair. 2003 ; 2 (5) : 581-591.
PMID 12713815
Human polymorphic variants of the NEIL1 DNA glycosylase.
Roy LM, Jaruga P, Wood TG, McCullough AK, Dizdaroglu M, Lloyd RS
The Journal of biological chemistry. 2007 ; 282 (21) : 15790-15798.
PMID 17389588
Association between cigarette smoking, APC mutations and the risk of developing sporadic colorectal adenomas and carcinomas.
Sareb&oring; M, Skjelbred CF, Breistein R, Lothe IM, Hagen PC, Bock G, Hansteen IL, Kure EH
BMC cancer. 2006 ; 6 : page 71.
PMID 16545110
Inactivating mutations of the human base excision repair gene NEIL1 in gastric cancer.
Shinmura K, Tao H, Goto M, Igarashi H, Taniguchi T, Maekawa M, Takezaki T, Sugimura H
Carcinogenesis. 2004 ; 25 (12) : 2311-2317.
PMID 15319300
A back-up glycosylase in Nth1 knock-out mice is a functional Nei (endonuclease VIII) homologue.
Takao M, Kanno S, Kobayashi K, Zhang QM, Yonei S, van der Horst GT, Yasui A
The Journal of biological chemistry. 2002 ; 277 (44) : 42205-42213.
PMID 12200441
The metabolic syndrome resulting from a knockout of the NEIL1 DNA glycosylase.
Vartanian V, Lowell B, Minko IG, Wood TG, Ceci JD, George S, Ballinger SW, Corless CL, McCullough AK, Lloyd RS
Proceedings of the National Academy of Sciences of the United States of America. 2006 ; 103 (6) : 1864-1869.
PMID 16446448
AP endonuclease-independent DNA base excision repair in human cells.
Wiederhold L, Leppard JB, Kedar P, Karimi-Busheri F, Rasouli-Nia A, Weinfeld M, Tomkinson AE, Izumi T, Prasad R, Wilson SH, Mitra S, Hazra TK
Molecular cell. 2004 ; 15 (2) : 209-220.
PMID 15260972
DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells.
Zhang QM, Yonekura S, Takao M, Yasui A, Sugiyama H, Yonei S
DNA repair. 2005 ; 4 (1) : 71-79.
PMID 15533839


This paper should be referenced as such :
Suzuki, M ; Shinmura, K ; Sugimura, H. NEIL1 (nei endonuclease VIII-like 1 (E
Atlas Genet Cytogenet Oncol Haematol. 2008;12(1):53-55.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)NEIL1   18448
Atlas Explorer : (Salamanque)NEIL1
Entrez_Gene (NCBI)NEIL1    nei like DNA glycosylase 1
AliasesFPG1; NEI1; hFPG1
GeneCards (Weizmann)NEIL1
Ensembl hg19 (Hinxton)ENSG00000140398 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000140398 [Gene_View]  ENSG00000140398 [Sequence]  chr15:75347039-75357115 [Contig_View]  NEIL1 [Vega]
ICGC DataPortalENSG00000140398
TCGA cBioPortalNEIL1
Genatlas (Paris)NEIL1
SOURCE (Princeton)NEIL1
Genetics Home Reference (NIH)NEIL1
Genomic and cartography
GoldenPath hg38 (UCSC)NEIL1  -     chr15:75347039-75357115 +  15q24.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)NEIL1  -     15q24.2   [Description]    (hg19-Feb_2009)
GoldenPathNEIL1 - 15q24.2 [CytoView hg19]  NEIL1 - 15q24.2 [CytoView hg38]
Genome Data Viewer NCBINEIL1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB079068 AK026055 AK026216 AK097008 AK128372
RefSeq transcript (Entrez)NM_001256552 NM_001352519 NM_001352520 NM_024608
Consensus coding sequences : CCDS (NCBI)NEIL1
Gene ExpressionNEIL1 [ NCBI-GEO ]   NEIL1 [ EBI - ARRAY_EXPRESS ]   NEIL1 [ SEEK ]   NEIL1 [ MEM ]
Gene Expression Viewer (FireBrowse)NEIL1 [ Firebrowse - Broad ]
GenevisibleExpression of NEIL1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)79661
GTEX Portal (Tissue expression)NEIL1
Human Protein AtlasENSG00000140398-NEIL1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ96FI4   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ96FI4  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ96FI4
Catalytic activity : Enzyme3.2.2.- [ Enzyme-Expasy ]   3.2.2.-3.2.2.- [ IntEnz-EBI ]   3.2.2.- [ BRENDA ]   3.2.2.- [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)FPG_CAT (PS51068)   
Domains : Interpro (EBI)DNA_glyclase/AP_lyase_DNA-bd    Endonuclease-VIII_DNA-bd    FPG_cat    MutM-like_N-ter    Ribosomal_S13-like_H2TH   
Domain families : Pfam (Sanger)Fapy_DNA_glyco (PF01149)    Neil1-DNA_bind (PF09292)   
Domain families : Pfam (NCBI)pfam01149    pfam09292   
Domain families : Smart (EMBL)Fapy_DNA_glyco (SM00898)  H2TH (SM01232)  
Conserved Domain (NCBI)NEIL1
PDB (RSDB)1TDH    4NRV    5ITQ    5ITR    5ITT    5ITU    5ITX    5ITY   
PDB Europe1TDH    4NRV    5ITQ    5ITR    5ITT    5ITU    5ITX    5ITY   
PDB (PDBSum)1TDH    4NRV    5ITQ    5ITR    5ITT    5ITU    5ITX    5ITY   
PDB (IMB)1TDH    4NRV    5ITQ    5ITR    5ITT    5ITU    5ITX    5ITY   
Structural Biology KnowledgeBase1TDH    4NRV    5ITQ    5ITR    5ITT    5ITU    5ITX    5ITY   
SCOP (Structural Classification of Proteins)1TDH    4NRV    5ITQ    5ITR    5ITT    5ITU    5ITX    5ITY   
CATH (Classification of proteins structures)1TDH    4NRV    5ITQ    5ITR    5ITT    5ITU    5ITX    5ITY   
AlphaFold pdb e-kbQ96FI4   
Human Protein Atlas [tissue]ENSG00000140398-NEIL1 [tissue]
Protein Interaction databases
IntAct (EBI)Q96FI4
Ontologies - Pathways
Ontology : AmiGOdamaged DNA binding  DNA-(apurinic or apyrimidinic site) endonuclease activity  DNA-(apurinic or apyrimidinic site) endonuclease activity  nucleus  nucleus  nucleoplasm  nucleoplasm  chromosome  cytoplasm  microtubule organizing center  cytosol  base-excision repair  base-excision repair  base-excision repair, gap-filling  response to oxidative stress  protein C-terminus binding  zinc ion binding  hydrolase activity, acting on glycosyl bonds  DNA N-glycosylase activity  DNA N-glycosylase activity  negative regulation of nuclease activity  depyrimidination  nucleic acid phosphodiester bond hydrolysis  class I DNA-(apurinic or apyrimidinic site) endonuclease activity  
Ontology : EGO-EBIdamaged DNA binding  DNA-(apurinic or apyrimidinic site) endonuclease activity  DNA-(apurinic or apyrimidinic site) endonuclease activity  nucleus  nucleus  nucleoplasm  nucleoplasm  chromosome  cytoplasm  microtubule organizing center  cytosol  base-excision repair  base-excision repair  base-excision repair, gap-filling  response to oxidative stress  protein C-terminus binding  zinc ion binding  hydrolase activity, acting on glycosyl bonds  DNA N-glycosylase activity  DNA N-glycosylase activity  negative regulation of nuclease activity  depyrimidination  nucleic acid phosphodiester bond hydrolysis  class I DNA-(apurinic or apyrimidinic site) endonuclease activity  
REACTOMEQ96FI4 [protein]
REACTOME PathwaysR-HSA-9616334 [pathway]   
NDEx NetworkNEIL1
Atlas of Cancer Signalling NetworkNEIL1
Wikipedia pathwaysNEIL1
Orthology - Evolution
GeneTree (enSembl)ENSG00000140398
Phylogenetic Trees/Animal Genes : TreeFamNEIL1
Homologs : HomoloGeneNEIL1
Homology/Alignments : Family Browser (UCSC)NEIL1
Gene fusions - Rearrangements
Fusion : FusionHubCSPG4--NEIL1    MEGF6--NEIL1    NEIL1--CALML4    NEIL1--GRAMD1A    NEIL1--NEIL1    NEIL1--YWHAZ   
Fusion : QuiverNEIL1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerNEIL1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)NEIL1
Exome Variant ServerNEIL1
GNOMAD BrowserENSG00000140398
Varsome BrowserNEIL1
ACMGNEIL1 variants
Genomic Variants (DGV)NEIL1 [DGVbeta]
DECIPHERNEIL1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisNEIL1 
ICGC Data PortalNEIL1 
TCGA Data PortalNEIL1 
Broad Tumor PortalNEIL1
OASIS PortalNEIL1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICNEIL1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DNEIL1
Mutations and Diseases : HGMDNEIL1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)NEIL1
DoCM (Curated mutations)NEIL1
CIViC (Clinical Interpretations of Variants in Cancer)NEIL1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry NEIL1
NextProtQ96FI4 [Medical]
Target ValidationNEIL1
Huge Navigator NEIL1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDNEIL1
Pharm GKB GenePA38334
Clinical trialNEIL1
DataMed IndexNEIL1
PubMed99 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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