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Search results 1 to 100 out of 113 for Faap24

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0.054s
Type Details Score
Gene
Type: gene
Organism: human
Gene
Type: gene
Organism: cattle
Gene
Type: gene
Organism: chicken
Gene
Type: gene
Organism: zebrafish
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: frog, western clawed
Gene
Type: gene
Organism: rat
Gene
Type: gene
Organism: dog, domestic
Gene
Type: gene
Organism: chimpanzee
Protein Domain
Type: Family
Description: Fanconi anemia-associated protein of 24kDa (FAAP24) plays a role in DNA repair through recruitment of the FA core complex to damaged DNA. It regulates FANCD2 monoubiquitination upon DNA damage. When repressed, it induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents. It targets FANCM/FAAP24 complex to the DNA, preferentially to single strand DNA [].Fanconi anemia (FA) is a human disorder characterized by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. The FA complex repairs the interstrand cross-linking (ICL) lesions and coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesion synthesis, and homologous recombination. It is required for the monoubiquitylation of FANCD2 and FANCI heterodimer. The FA core complex consists of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FANCT (UBET2), FAAP100 and FAAP24 [, ].
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Ciccia A
Year: 2007
Journal: Mol Cell
Title: Identification of FAAP24, a Fanconi anemia core complex protein that interacts with FANCM.
Volume: 25
Issue: 3
Pages: 331-43
Publication
First Author: Yan Z
Year: 2010
Journal: Mol Cell
Title: A histone-fold complex and FANCM form a conserved DNA-remodeling complex to maintain genome stability.
Volume: 37
Issue: 6
Pages: 865-78
Publication
First Author: Bhattacharjee S
Year: 2017
Journal: Cell Commun Signal
Title: DNA damage response and cancer therapeutics through the lens of the Fanconi Anemia DNA repair pathway.
Volume: 15
Issue: 1
Pages: 41
Protein
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
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
Publication
First Author: Friedel RH
Year: 2007
Journal: Brief Funct Genomic Proteomic
Title: EUCOMM--the European conditional mouse mutagenesis program.
Volume: 6
Issue: 3
Pages: 180-5
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations for FANTOM2 data
Publication        
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
Publication        
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication
First Author: Gaudet P
Year: 2011
Journal: Brief Bioinform
Title: Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium.
Volume: 12
Issue: 5
Pages: 449-62
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: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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 Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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 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 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
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Protein
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
Publication
First Author: Lorenz A
Year: 2012
Journal: Science
Title: The fission yeast FANCM ortholog directs non-crossover recombination during meiosis.
Volume: 336
Issue: 6088
Pages: 1585-8
Protein Domain
Type: Family
Description: Centromere protein X (CENP-X) is a component of several different complexes, including the multisubunit FA complex, the heterotetrameric CENP-T-W-S-X complex and the APITD1/CENPS complex. The Fanconi anemia (FA) core complex is involved in DNA damage repair and genome maintenance. The FA complex is composed of CENPS, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9, FANCM, FAAP24 and CENPX. Interacts with CENPS, FANCM and FAAP24 [, ]. Inner kinetochore subunit mhf2 is the dsDNA-binding component of the FANCM-MHF complex, important for gene conversion at blocked replication forks []and non-crossover recombination during mitosis and meiosis [].The CENP-T-W-S-X complex binds, supercoils DNA and plays an important role in kinetochore assembly [].The APITD1/CENPS complex is composed of at least of CENP-S and CENP-X and is essential for the stable assembly of the outer kinetchore [].
Protein
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 660  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 412  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 43  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 461  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 283  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
Protein Domain
Type: Family
Description: Fanconi anemia (FA) is a human disorder characterized by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. The FA complex repairs the interstrand cross-linking (ICL) lesions and coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesion synthesis, and homologous recombination. It is required for the monoubiquitylation of FANCD2 and FANCI heterodimer. The FA core complex consists of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FANCT (UBET2), FAAP100 and FAAP24 [, ].This entry represents FANCC [].
Protein Domain
Type: Family
Description: Fanconi anemia (FA) is a human disorder characterized by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. The FA complex repairs the interstrand cross-linking (ICL) lesions and coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesion synthesis, and homologous recombination. It is required for the monoubiquitylation of FANCD2 and FANCI heterodimer. The FA core complex consists of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FANCT (UBET2), FAAP100 and FAAP24 [, ].This entry represents FANCA [].
Protein Domain
Type: Domain
Description: Fanconi anemia (FA) is a human disorder characterized by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. The FA complex repairs the interstrand cross-linking (ICL) lesions and coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesion synthesis, and homologous recombination. It is required for the monoubiquitylation of FANCD2 and FANCI heterodimer. The FA core complex consists of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FANCT (UBET2), FAAP100 and FAAP24 [, ].This entry represents the N-terminal domain of FANCA.
Protein Domain
Type: Family
Description: Fanconi anemia (FA) is a human disorder characterized by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. The FA complex repairs the interstrand cross-linking (ICL) lesions and coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesion synthesis, and homologous recombination. It is required for the monoubiquitylation of FANCD2 and FANCI heterodimer. The FA core complex consists of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FANCT (UBET2), FAAP100 and FAAP24 [, ].The FA group E protein (FANCE) has an important role in DNA repair, functioning as the FANCD2-binding protein in the FA core complex [].
Protein
Organism: Mus musculus/domesticus
Length: 1439  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1439  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 481  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 771  
Fragment?: true
Publication
First Author: Amano M
Year: 2009
Journal: J Cell Biol
Title: The CENP-S complex is essential for the stable assembly of outer kinetochore structure.
Volume: 186
Issue: 2
Pages: 173-82
Publication
First Author: Singh TR
Year: 2010
Journal: Mol Cell
Title: MHF1-MHF2, a histone-fold-containing protein complex, participates in the Fanconi anemia pathway via FANCM.
Volume: 37
Issue: 6
Pages: 879-86
Protein
Organism: Mus musculus/domesticus
Length: 879  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
Publication
First Author: Alpi A
Year: 2007
Journal: Mol Cell Biol
Title: UBE2T, the Fanconi anemia core complex, and FANCD2 are recruited independently to chromatin: a basis for the regulation of FANCD2 monoubiquitination.
Volume: 27
Issue: 24
Pages: 8421-30
Publication
First Author: Meetei AR
Year: 2003
Journal: Nat Genet
Title: A novel ubiquitin ligase is deficient in Fanconi anemia.
Volume: 35
Issue: 2
Pages: 165-70
Publication
First Author: Meetei AR
Year: 2004
Journal: Nat Genet
Title: X-linked inheritance of Fanconi anemia complementation group B.
Volume: 36
Issue: 11
Pages: 1219-24
Publication
First Author: Sato K
Year: 2012
Journal: Nucleic Acids Res
Title: DNA robustly stimulates FANCD2 monoubiquitylation in the complex with FANCI.
Volume: 40
Issue: 10
Pages: 4553-61
Publication
First Author: Ling C
Year: 2007
Journal: EMBO J
Title: FAAP100 is essential for activation of the Fanconi anemia-associated DNA damage response pathway.
Volume: 26
Issue: 8
Pages: 2104-14
Protein Domain
Type: Family
Description: Fanconi anemia (FA) is a human disorder characterized by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. The FA complex repairs the interstrand cross-linking (ICL) lesions and coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesion synthesis, and homologous recombination. It is required for the monoubiquitylation of FANCD2 and FANCI heterodimer. The FA core complex consists of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FANCT (UBET2), FAAP100 and FAAP24 [, ].FANCL is an ubiquitin ligase that mediates monoubiquitination of FANCD2, a key step in the repair of interstrand DNA crosslinks (ICLs) in the Fanconi anemia (FA) pathway [, ]. In humans, defects in FANCL are the cause of Fanconi anemia complementation group L (FANCL). FANCL is a disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair [, ].
Protein Domain
Type: Family
Description: Fanconi anemia-associated protein of 100kDa (FAAP100) is component of the Fanconi anemia (FA) core complex, which plays a central role in FA-associated DNA damage response. FAAP100 is essential for the stability and function of the complex [].Fanconi anemia (FA) is a human disorder characterized by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. The FA complex repairs the interstrand cross-linking (ICL) lesions and coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesion synthesis, and homologous recombination. It is required for the monoubiquitylation of FANCD2 and FANCI heterodimer. The FA core complex consists of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FANCT (UBET2), FAAP100 and FAAP24 [, ].
Protein Domain
Type: Family
Description: Fanconi anemia (FA) is a human disorder characterized by cancer susceptibility and cellular sensitivity to DNA crosslinks and other damages. The FA complex repairs the interstrand cross-linking (ICL) lesions and coordinates activities of the downstream DNA repair pathway including nucleotide excision repair, translesion synthesis, and homologous recombination. It is required for the monoubiquitylation of FANCD2 and FANCI heterodimer. The FA core complex consists of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FANCT (UBET2), FAAP100 and FAAP24 [, ].Fanconi anemia group F protein (FANCF) is a component of the FA core complex [, ]. FANCF regulates its own expression by methylation at both mRNA and protein levels. Methylation-induced inactivation of FANCF has an important role on the occurrence of ovarian cancers by disrupting the FA-BRCA pathway [].This entry also includes homologues from plants.
Protein
Organism: Mus musculus/domesticus
Length: 384  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 484  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false