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Search results 1 to 90 out of 90 for Neil2

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Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Gene
252969 | NEIL2
Type: gene
Organism: human
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Gene
100135209 | neil2
Type: gene
Organism: frog, western clawed
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Gene
305957 | Neil2
Type: gene
Organism: rat
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Gene
486078 | NEIL2
Type: gene
Organism: dog, domestic
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Gene
463992 | NEIL2
Type: gene
Organism: chimpanzee
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Gene
444987 | NEIL2
Type: gene
Organism: cattle
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Gene
422037 | NEIL2
Type: gene
Organism: chicken
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Gene
696647 | NEIL2
Type: gene
Organism: macaque, rhesus
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Protein Coding Gene
MGI:2686058 | Neil2
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
33932404 | J:316229
 
First Author: Tapryal N
Year: 2021
Journal: J Biol Chem
Title: Intrapulmonary administration of purified NEIL2 abrogates NF-κB-mediated inflammation.
Volume: 296
Pages: 100723
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Publication
31566562 | J:281569
   
First Author: Han D
Year: 2019
Journal: Elife
Title: NEIL1 and NEIL2 DNA glycosylases protect neural crest development against mitochondrial oxidative stress.
Volume: 8
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Publication
34857879 | J:331155
First Author: Hildrestrand GA
Year: 2021
Journal: Commun Biol
Title: NEIL1 and NEIL2 DNA glycosylases modulate anxiety and learning in a cooperative manner in mice.
Volume: 4
Issue: 1
Pages: 1354
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Publication
20175991 | J:158820
First Author: Grin IR
Year: 2010
Journal: Biochem Biophys Res Commun
Title: Inactivation of NEIL2 DNA glycosylase by pyridoxal phosphate reveals a loop important for substrate binding.
Volume: 394
Issue: 1
Pages: 100-5
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Publication
32872214 | J:306339
 
First Author: Sayed IM
Year: 2020
Journal: Cells
Title: The DNA Glycosylase NEIL2 Suppresses Fusobacterium-Infection-Induced Inflammation and DNA Damage in Colonic Epithelial Cells.
Volume: 9
Issue: 9
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Publication
15725623 | J:96949
First Author: Conlon KA
Year: 2005
Journal: DNA Repair (Amst)
Title: The murine DNA glycosylase NEIL2 (mNEIL2) and human DNA polymerase beta bind microtubules in situ and in vitro.
Volume: 4
Issue: 4
Pages: 419-31
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GXD Expression
GXD Expression
 
Probe: MGI:7544974
Assay Type: Immunohistochemistry
Annotation Date: 2023-11-01
Strength: Present
Sex: Female
Emaps: EMAPS:1657819
Pattern: Not Specified
Stage: TS19
Assay Id: MGI:7545030
Age: embryonic day 11.5
Note: The proportion of Neil2 positive cells was significantly decreased compared with the wild-type (quantified in Fig 9B).
Specimen Label: 9A E11.5 -/-
Detected: true
Specimen Num: 2
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GXD Expression
GXD Expression
 
Probe: MGI:7544974
Assay Type: Immunohistochemistry
Annotation Date: 2023-11-01
Strength: Present
Sex: Female
Emaps: EMAPS:1657820
Pattern: Not Specified
Stage: TS20
Assay Id: MGI:7545030
Age: embryonic day 12.5
Note: The proportion of Neil2 positive cells was significantly decreased compared with the wild-type (quantified in Fig 9B).
Specimen Label: 9A E12.5 -/-
Detected: true
Specimen Num: 4
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Publication
26245904 | J:225791
First Author: Chakraborty A
Year: 2015
Journal: J Biol Chem
Title: Neil2-null Mice Accumulate Oxidized DNA Bases in the Transcriptionally Active Sequences of the Genome and Are Susceptible to Innate Inflammation.
Volume: 290
Issue: 41
Pages: 24636-48
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Publication
16920106 | J:112297
First Author: Grin IR
Year: 2006
Journal: FEBS Lett
Title: Deoxyribophosphate lyase activity of mammalian endonuclease VIII-like proteins.
Volume: 580
Issue: 20
Pages: 4916-22
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Publication
28663564 | J:255084
First Author: Rolseth V
Year: 2017
Journal: Sci Rep
Title: No cancer predisposition or increased spontaneous mutation frequencies in NEIL DNA glycosylases-deficient mice.
Volume: 7
Issue: 1
Pages: 4384
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Protein Coding Gene
MGP_CAROLIEiJ_G0019402 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0021458 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0021417 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0021393 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0021423 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0021200 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_2686058 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0021862 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0020717 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0021167 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0021290 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0021269 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0021365 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0021298 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0021885 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0020461 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0020770 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0030420 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0020294 | -
Type: protein_coding_gene
Organism: Mus spretus
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GXD Expression
GXD Expression
   
Probe: MGI:7544974
Assay Type: Immunohistochemistry
Annotation Date: 2023-11-01
Strength: Present
Sex: Female
Emaps: EMAPS:1657819
Pattern: Not Specified
Stage: TS19
Assay Id: MGI:7545030
Age: embryonic day 11.5
Specimen Label: 9A E11.5 +/+
Detected: true
Specimen Num: 1
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GXD Expression
GXD Expression
   
Probe: MGI:7544974
Assay Type: Immunohistochemistry
Annotation Date: 2023-11-01
Strength: Present
Sex: Female
Emaps: EMAPS:1657820
Pattern: Not Specified
Stage: TS20
Assay Id: MGI:7545030
Age: embryonic day 12.5
Specimen Label: 9A E12.5 +/+
Detected: true
Specimen Num: 3
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Publication
30745429 | J:272594
 
First Author: Nakamoto C
Year: 2019
Journal: Development
Title: Nell2 regulates the contralateral-versus-ipsilateral visual projection as a domain-specific positional cue.
Volume: 146
Issue: 4
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Publication
24366543 | J:222136
First Author: Fukutomi T
Year: 2014
Journal: Mol Cell Biol
Title: Kinetic, thermodynamic, and structural characterizations of the association between Nrf2-DLGex degron and Keap1.
Volume: 34
Issue: 5
Pages: 832-46
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Publication
16581765 | J:240280
First Author: Tong KI
Year: 2006
Journal: Mol Cell Biol
Title: Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model.
Volume: 26
Issue: 8
Pages: 2887-900
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Publication
37563658 | J:340875
First Author: Zhou Z
Year: 2023
Journal: J Ovarian Res
Title: Fance deficiency inhibits primordial germ cell proliferation associated with transcription-replication conflicts accumulate and DNA repair defects.
Volume: 16
Issue: 1
Pages: 160
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Publication
- | J:66660
       
First Author: Mouse Genome Database and National Center for Biotechnology Information Editorial Staff Collaboration
Year: 2001
Title: LocusLink Collaboration
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Publication
- | J:342608
       
First Author: GO Central curators, GOA curators, Rhea curators
Year: 2020
Title: Automatic Gene Ontology annotation based on Rhea mapping
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Publication
- | J:72245
       
First Author: GOA curators, MGI curators
Year: 2001
Title: Gene Ontology annotation based on Enzyme Commission mapping
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Publication
- | J:84900
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Journal: Database Download
Title: Integrating Computational Gene Models into the Mouse Genome Informatics (MGI) Database
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Publication
- | J:188991
     
First Author: The Jackson Laboratory
Year: 2012
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by The Jackson Laboratory
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Publication
- | J:238766
     
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
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Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
15339932 | -
First Author: Das A
Year: 2004
Journal: J Biol Chem
Title: Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein.
Volume: 279
Issue: 45
Pages: 47132-8
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GXD Expression
GXD Expression
 
Probe: MGI:6694992
Assay Type: Immunohistochemistry
Annotation Date: 2023-11-01
Strength: Present
Sex: Female
Emaps: EMAPS:1657819
Pattern: Not Specified
Stage: TS19
Assay Id: MGI:7544998
Age: embryonic day 11.5
Note: The proportion of Neil2 positive cells was significantly decreased compared with the wild-type (quantified in Fig 9B).
Specimen Label: 9A E11.5 -/-
Detected: true
Specimen Num: 38
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GXD Expression
GXD Expression
 
Probe: MGI:6694992
Assay Type: Immunohistochemistry
Annotation Date: 2023-11-01
Strength: Present
Sex: Female
Emaps: EMAPS:1657820
Pattern: Not Specified
Stage: TS20
Assay Id: MGI:7544998
Age: embryonic day 12.5
Note: The proportion of Neil2 positive cells was significantly decreased compared with the wild-type (quantified in Fig 9B).
Specimen Label: 9A E12.5 -/-
Detected: true
Specimen Num: 40
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Protein
Q6R2P8
Organism: Mus musculus/domesticus
Length: 329  
Fragment?: false
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Publication
20185759 | J:158756
First Author: Liu M
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo.
Volume: 107
Issue: 11
Pages: 4925-30
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Publication
19782007 | J:153965
First Author: Mori H
Year: 2009
Journal: DNA Repair (Amst)
Title: Deficiency of the oxidative damage-specific DNA glycosylase NEIL1 leads to reduced germinal center B cell expansion.
Volume: 8
Issue: 11
Pages: 1328-32
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Publication
23127499 | J:318159
First Author: Bacsi A
Year: 2013
Journal: DNA Repair (Amst)
Title: Down-regulation of 8-oxoguanine DNA glycosylase 1 expression in the airway epithelium ameliorates allergic lung inflammation.
Volume: 12
Issue: 1
Pages: 18-26
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Protein Domain
IPR000214 | Znf_DNA_glyclase/AP_lyase
Type: Domain
Description: Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents DNA glycosylase/AP lyase enzymes that are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. These enzymes are primarily from bacteria, and have both DNA glycosylase activity () and AP lyase activity (). Examples include formamidopyrimidine-DNA glycosylases (Fpg; MutM) and endonuclease VIII (Nei). These enzymes contain a zinc finger domain that is important for DNA-binding.Formamidopyrimidine-DNA glycosylases (Fpg, MutM) is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidation-damaged bases (N-glycosylase activity; ) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity; ). Fpg has a preference for oxidised purines, excising oxidized purine bases such as 7,8-dihydro-8-oxoguanine (8-oxoG). ITs AP (apurinic/apyrimidinic) lyase activity introduces nicks in the DNA strand, cleaving 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. Fpg is a monomer composed of 2 domains connected by a flexible hinge []. The two DNA-binding motifs (a zinc finger and the helix-two-turns-helix motifs) suggest that the oxidized base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes []. Fpg binds one ion of zinc at the C terminus, which contains four conserved and essential cysteines [, ].Endonuclease VIII (Nei) has the same enzyme activities as Fpg above (, ), but with a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine []. Three human homologues of Escherichia coli Nei have been identified, called Nei-like (NEIL) enzyme. NEIL2 (Nei-like-2) shares structural features and reaction mechanism with E. coli Nei (and Fpg), but it contains a C4-type zinc finger in place of the CHCC-type found in Nei and Fpg []. By contrast, the structure of NEIL1 exhibits the same overall fold as E. coli Nei; however, the β-hairpin zinc finger found in other Fpg/Nei family members is replaced by a structural motif composed of two antiparallel β-strands that mimics a zinc finger but lacks the loops that harbour the zinc-binding residues and, therefore, does not coordinate zinc []. This entry identifies the zinc finger in NEIL2, but not the "zincless finger"in NEIL1.
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Publication
7704272 | -
 
First Author: Duwat P
Year: 1995
Journal: Microbiology
Title: Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein.
Volume: 141 ( Pt 2)
Pages: 411-7
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Publication
15232006 | -
First Author: Doublié S
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity.
Volume: 101
Issue: 28
Pages: 10284-9
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Protein
Q8K203
Organism: Mus musculus/domesticus
Length: 606  
Fragment?: false
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Publication
8473347 | -
First Author: O'Connor TR
Year: 1993
Journal: J Biol Chem
Title: Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role.
Volume: 268
Issue: 12
Pages: 9063-70
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Publication
10921868 | -
First Author: Sugahara M
Year: 2000
Journal: EMBO J
Title: Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8.
Volume: 19
Issue: 15
Pages: 3857-69
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Publication
12665246 | -
First Author: Matthews JM
Year: 2002
Journal: IUBMB Life
Title: Zinc fingers--folds for many occasions.
Volume: 54
Issue: 6
Pages: 351-5
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Publication
17210253 | -
First Author: Gamsjaeger R
Year: 2007
Journal: Trends Biochem Sci
Title: Sticky fingers: zinc-fingers as protein-recognition motifs.
Volume: 32
Issue: 2
Pages: 63-70
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Publication
15963892 | -
First Author: Hall TM
Year: 2005
Journal: Curr Opin Struct Biol
Title: Multiple modes of RNA recognition by zinc finger proteins.
Volume: 15
Issue: 3
Pages: 367-73
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Publication
15718139 | -
First Author: Brown RS
Year: 2005
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: getting a grip on RNA.
Volume: 15
Issue: 1
Pages: 94-8
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Publication
10529348 | -
First Author: Klug A
Year: 1999
Journal: J Mol Biol
Title: Zinc finger peptides for the regulation of gene expression.
Volume: 293
Issue: 2
Pages: 215-8
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Publication
11179890 | -
First Author: Laity JH
Year: 2001
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: new insights into structural and functional diversity.
Volume: 11
Issue: 1
Pages: 39-46
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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