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Search results 101 to 200 out of 215 for Dap3

0.043s
Type Details Score
Publication      
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
Publication
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication        
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
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 Genome 430 2.0 Array Platform
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
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
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: RIKEN Data Curation in Mouse Genome Informatics
Publication      
First Author: The Jackson Laboratory
Year: 2012
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by The Jackson Laboratory
Publication
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
Publication
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Gene
Type: gene
Organism: rat
Gene
Type: gene
Organism: dog, domestic
Gene
Type: gene
Organism: chimpanzee
Gene
Type: gene
Organism: cattle
Gene
Type: gene
Organism: zebrafish
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: frog, western clawed
Gene
Type: gene
Organism: frog, African clawed
Gene
Type: gene
Organism: frog, African clawed
Allele  
Name: DAP3 binding cell death enhancer 1; wild type
Allele Type: Not Specified
Allele
Name: DAP3 binding cell death enhancer 1; endonuclease-mediated mutation 1, GemPharmatech
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Publication  
First Author: Huynh H
Year: 2023
Journal: J Mol Cell Cardiol
Title: DELE1 is protective for mitochondrial cardiomyopathy.
Volume: 175
Pages: 44-48
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1610528
Stage: TS28
Assay Id: MGI:7620340
Age: postnatal day 12
Specimen Label: Ctrl
Detected: true
Specimen Num: 1
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1610528
Stage: TS28
Assay Id: MGI:7620340
Age: postnatal day 12
Specimen Label: cKO
Detected: true
Specimen Num: 2
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1610519
Stage: TS19
Assay Id: MGI:7620346
Age: embryonic day 11.5
Specimen Label: Ctrl
Detected: true
Specimen Num: 1
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1610519
Stage: TS19
Assay Id: MGI:7620346
Age: embryonic day 11.5
Specimen Label: cKO
Detected: false
Specimen Num: 2
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1610519
Stage: TS19
Assay Id: MGI:7620346
Age: embryonic day 11.5
Specimen Label: PKO
Detected: true
Specimen Num: 3
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1610519
Stage: TS19
Assay Id: MGI:7620346
Age: embryonic day 11.5
Specimen Label: dcKO
Detected: false
Specimen Num: 4
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1610528
Stage: TS28
Assay Id: MGI:7620354
Age: postnatal day 10
Specimen Label: Ctrl
Detected: true
Specimen Num: 1
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1610528
Stage: TS28
Assay Id: MGI:7620354
Age: postnatal day 10
Specimen Label: cKO
Detected: false
Specimen Num: 2
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1610528
Stage: TS28
Assay Id: MGI:7620354
Age: postnatal day 10
Specimen Label: TKO
Detected: true
Specimen Num: 3
GXD Expression      
Probe: MGI:7620326
Assay Type: RT-PCR
Annotation Date: 2024-04-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1610528
Stage: TS28
Assay Id: MGI:7620354
Age: postnatal day 10
Specimen Label: dcKO
Detected: false
Specimen Num: 4
Allele  
Name: DAP3 binding cell death enhancer 1; gene trap OST38933, Lexicon Genetics
Allele Type: Gene trapped
Allele  
Name: DAP3 binding cell death enhancer 1; gene trap OST38957, Lexicon Genetics
Allele Type: Gene trapped
Allele  
Name: DAP3 binding cell death enhancer 1; gene trap EUCJ0183g07, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
Allele
Name: DAP3 binding cell death enhancer 1; endonuclease-mediated mutation 2, Institute of Molecular Genetics
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Allele
Name: DAP3 binding cell death enhancer 1; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Allele
Name: DAP3 binding cell death enhancer 1; endonuclease-mediated mutation 1, Xi Fang
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Allele
Name: DAP3 binding cell death enhancer 1; endonuclease-mediated mutation 1, Cyagen Biosciences
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Allele
Name: DAP3 binding cell death enhancer 1; endonuclease-mediated mutation 2, Cyagen Biosciences
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
Protein
Organism: Mus musculus/domesticus
Length: 977  
Fragment?: false
Allele  
Name: DAP3 binding cell death enhancer 1; gene trap IST11133A10, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
Strain
Attribute String: coisogenic, targeted mutation
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Genotype
Symbol: Dele1/Dele1
Background: C57BL/6N-Dele1/Ccpcz
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Dele1/Dele1 Tg(myl7.L-cre)1118Tmhn/?
Background: involves: C57BL/6NCrl * MF1
Zygosity: cn
Has Mutant Allele: true
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Allele
Name: transgene insertion EI119, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Reporter
Genotype
Symbol: Dele1/Dele1 Ptpmt1/Ptpmt1 Tg(myl7.L-cre)1118Tmhn/?
Background: involves: 129S1/Sv * 129X1/SvJ * C57BL/6NCrl * MF1
Zygosity: cn
Has Mutant Allele: true
Genotype
Symbol: Dele1/Dele1 Tafazzin/Tafazzin Tg(myl7.L-cre)1118Tmhn/?
Background: involves: C57BL/6NCrl * MF1
Zygosity: cn
Has Mutant Allele: true
Strain
Attribute String: mutant stock, transgenic
Publication
First Author: Li HM
Year: 2009
Journal: Cell Death Differ
Title: IPS-1 is crucial for DAP3-mediated anoikis induction by caspase-8 activation.
Volume: 16
Issue: 12
Pages: 1615-21
Publication
First Author: Suzuki T
Year: 2001
Journal: J Biol Chem
Title: Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28 S small subunit.
Volume: 276
Issue: 35
Pages: 33181-95
Protein Domain
Type: Family
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].This entry represents a family of conserved proteins which were originally described as death-associated-protein-3 (DAP-3). The proteins carry a P-loop DNA-binding motif, and induce apoptosis []. DAP3 has been shown to be a pro-apoptotic factor in the mitochondrial matrix []and to be crucial for mitochondrial biogenesis and so has also been designated as MRP-S29 (mitochondrial ribosomal protein subunit 29).
Protein Domain
Type: Family
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].This entry represents a family of conserved proteins which were originally described as death-associated-protein-3 (DAP-3). The proteins carry a P-loop DNA-binding motif, and induce apoptosis []. DAP3 has been shown to be a pro-apoptotic factor in the mitochondrial matrix []and to be crucial for mitochondrial biogenesis and so has also been designated as MRP-S29 (mitochondrial ribosomal protein subunit 29).
Protein
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 396  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true