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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)

Identity

Other namesFLJ22402
FPG1
hFPG1
NEH1
NEI1
HGNC (Hugo) NEIL1
LocusID (NCBI) 79661
Atlas_Id 41519
Location 15q24.2  [Link to chromosome band 15q24]
Location_base_pair Starts at 75639960 and ends at 75647592 bp from pter ( according to hg19-Feb_2009)  [Mapping NEIL1.png]
Fusion genes
(updated 2016)
NEIL1 (15q24.2) / NEIL1 (15q24.2)

DNA/RNA

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.

Protein

 
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

Note
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.
  

Bibliography

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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
NEIL1 excises 3' end proximal oxidative DNA lesions resistant to cleavage by NTH1 and OGG1.
Parsons JL, Zharkov DO, Dianov GL
Nucleic acids research. 2005 ; 33 (15) : 4849-4856.
PMID 16129732
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 
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
 

Citation

This paper should be referenced as such :
Suzuki, M ; Shinmura, K ; Sugimura, H. NEIL1 (nei endonuclease VIII-like 1 (E
coli))
Atlas Genet Cytogenet Oncol Haematol. 2008;12(1):53-55.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/NEIL1ID41519ch15q24.html


External links

Nomenclature
HGNC (Hugo)NEIL1   18448
Cards
AtlasNEIL1ID41519ch15q24
Entrez_Gene (NCBI)NEIL1  79661  nei like DNA glycosylase 1
AliasesFPG1; NEI1; hFPG1
GeneCards (Weizmann)NEIL1
Ensembl hg19 (Hinxton)ENSG00000140398 [Gene_View]  chr15:75639960-75647592 [Contig_View]  NEIL1 [Vega]
Ensembl hg38 (Hinxton)ENSG00000140398 [Gene_View]  chr15:75639960-75647592 [Contig_View]  NEIL1 [Vega]
ICGC DataPortalENSG00000140398
TCGA cBioPortalNEIL1
AceView (NCBI)NEIL1
Genatlas (Paris)NEIL1
WikiGenes79661
SOURCE (Princeton)NEIL1
Genomic and cartography
GoldenPath hg19 (UCSC)NEIL1  -     chr15:75639960-75647592 +  15q33.33   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)NEIL1  -     15q33.33   [Description]    (hg38-Dec_2013)
EnsemblNEIL1 - 15q33.33 [CytoView hg19]  NEIL1 - 15q33.33 [CytoView hg38]
Mapping of homologs : NCBINEIL1 [Mapview hg19]  NEIL1 [Mapview hg38]
OMIM608844   
Gene and transcription
Genbank (Entrez)AB079068 AK026055 AK026216 AK097008 AK128372
RefSeq transcript (Entrez)NM_001256552 NM_024608
RefSeq genomic (Entrez)NC_000015 NC_018926 NT_010194 NW_004929398
Consensus coding sequences : CCDS (NCBI)NEIL1
Cluster EST : UnigeneHs.512732 [ NCBI ]
CGAP (NCI)Hs.512732
Alternative Splicing GalleryENSG00000140398
Gene ExpressionNEIL1 [ NCBI-GEO ]   NEIL1 [ EBI - ARRAY_EXPRESS ]   NEIL1 [ SEEK ]   NEIL1 [ MEM ]
Gene Expression Viewer (FireBrowse)NEIL1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)79661
GTEX Portal (Tissue expression)NEIL1
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ96FI4 (Uniprot)
NextProtQ96FI4  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ96FI4
Splice isoforms : SwissVarQ96FI4 (Swissvar)
Catalytic activity : Enzyme3.2.2.- [ Enzyme-Expasy ]   3.2.2.-3.2.2.- [ IntEnz-EBI ]   3.2.2.- [ BRENDA ]   3.2.2.- [ KEGG ]   
PhosPhoSitePlusQ96FI4
Domaine pattern : Prosite (Expaxy)FPG_CAT (PS51068)   
Domains : Interpro (EBI)DNA_glyclase/AP_lyase_DNA-bd    Endonuclease-VIII_DNA-bd    FPG_cat    Ribosomal_S13-like_H2TH   
Domain families : Pfam (Sanger)Fapy_DNA_glyco (PF01149)    H2TH (PF06831)    Neil1-DNA_bind (PF09292)   
Domain families : Pfam (NCBI)pfam01149    pfam06831    pfam09292   
Domain families : Smart (EMBL)Fapy_DNA_glyco (SM00898)  
DMDM Disease mutations79661
Blocks (Seattle)NEIL1
PDB (SRS)1TDH    4NRV   
PDB (PDBSum)1TDH    4NRV   
PDB (IMB)1TDH    4NRV   
PDB (RSDB)1TDH    4NRV   
Structural Biology KnowledgeBase1TDH    4NRV   
SCOP (Structural Classification of Proteins)1TDH    4NRV   
CATH (Classification of proteins structures)1TDH    4NRV   
SuperfamilyQ96FI4
Human Protein AtlasENSG00000140398
Peptide AtlasQ96FI4
HPRD12314
IPIIPI00305213   IPI00746550   
Protein Interaction databases
DIP (DOE-UCLA)Q96FI4
IntAct (EBI)Q96FI4
FunCoupENSG00000140398
BioGRIDNEIL1
STRING (EMBL)NEIL1
ZODIACNEIL1
Ontologies - Pathways
QuickGOQ96FI4
Ontology : AmiGOdamaged DNA binding  DNA-(apurinic or apyrimidinic site) lyase activity  nucleus  nucleoplasm  chromosome  cytoplasm  microtubule organizing center  base-excision repair  nucleotide-excision repair  response to oxidative stress  protein C-terminus binding  zinc ion binding  hydrolase activity, acting on glycosyl bonds  DNA N-glycosylase activity  negative regulation of nuclease activity  depyrimidination  
Ontology : EGO-EBIdamaged DNA binding  DNA-(apurinic or apyrimidinic site) lyase activity  nucleus  nucleoplasm  chromosome  cytoplasm  microtubule organizing center  base-excision repair  nucleotide-excision repair  response to oxidative stress  protein C-terminus binding  zinc ion binding  hydrolase activity, acting on glycosyl bonds  DNA N-glycosylase activity  negative regulation of nuclease activity  depyrimidination  
Pathways : KEGGBase excision repair   
REACTOMEQ96FI4 [protein]
REACTOME PathwaysR-HSA-5649702 APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway [pathway]
REACTOME PathwaysR-HSA-110329 Cleavage of the damaged pyrimidine [pathway]
REACTOME PathwaysR-HSA-110328 Recognition and association of DNA glycosylase with site containing an affected pyrimidine [pathway]
NDEx Network
Atlas of Cancer Signalling NetworkNEIL1
Wikipedia pathwaysNEIL1
Orthology - Evolution
OrthoDB79661
GeneTree (enSembl)ENSG00000140398
Phylogenetic Trees/Animal Genes : TreeFamNEIL1
Homologs : HomoloGeneNEIL1
Homology/Alignments : Family Browser (UCSC)NEIL1
Gene fusions - Rearrangements
Polymorphisms : SNP, variants
NCBI Variation ViewerNEIL1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)NEIL1
dbVarNEIL1
ClinVarNEIL1
1000_GenomesNEIL1 
Exome Variant ServerNEIL1
ExAC (Exome Aggregation Consortium)NEIL1 (select the gene name)
Genetic variants : HAPMAP79661
Genomic Variants (DGV)NEIL1 [DGVbeta]
Mutations
ICGC Data PortalNEIL1 
TCGA Data PortalNEIL1 
Broad Tumor PortalNEIL1
OASIS PortalNEIL1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICNEIL1 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch NEIL1
DgiDB (Drug Gene Interaction Database)NEIL1
DoCM (Curated mutations)NEIL1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)NEIL1 (select a term)
intoGenNEIL1
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
Diseases
DECIPHER (Syndromes)15:75639960-75647592  ENSG00000140398
CONAN: Copy Number AnalysisNEIL1 
Mutations and Diseases : HGMDNEIL1
OMIM608844   
MedgenNEIL1
Genetic Testing Registry NEIL1
NextProtQ96FI4 [Medical]
TSGene79661
GENETestsNEIL1
Huge Navigator NEIL1 [HugePedia]
snp3D : Map Gene to Disease79661
BioCentury BCIQNEIL1
ClinGenNEIL1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD79661
Chemical/Pharm GKB GenePA38334
Clinical trialNEIL1
Miscellaneous
canSAR (ICR)NEIL1 (select the gene name)
Probes
Litterature
PubMed67 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineNEIL1
EVEXNEIL1
GoPubMedNEIL1
iHOPNEIL1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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