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Search results 101 to 171 out of 171 for Rad17

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Type Details Score
Allele    
Name: RAD17 checkpoint clamp loader component; wild type
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap OST122844, Lexicon Genetics
Allele Type: Gene trapped
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap OST201553, Lexicon Genetics
Allele Type: Gene trapped
Allele
Name: RAD17 checkpoint clamp loader component; endonuclease-mediated mutation 1, GemPharmatech
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
Allele
Name: RAD17 checkpoint clamp loader component; targeted mutation 1, Alex Maas
Allele Type: Targeted
Attribute String: Null/knockout
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap OST230347, Lexicon Genetics
Allele Type: Gene trapped
Allele
Name: RAD17 checkpoint clamp loader component; targeted mutation 1, Velocigene
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap OST85074, Lexicon Genetics
Allele Type: Gene trapped
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap OST296068, Lexicon Genetics
Allele Type: Gene trapped
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap OST426300, Lexicon Genetics
Allele Type: Gene trapped
Publication
First Author: Yong W
Year: 2007
Journal: J Biol Chem
Title: Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia mutated (ATM)-mediated cell cycle arrest.
Volume: 282
Issue: 20
Pages: 14690-4
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap PST7532, Mammalian Functional Genomics Centre
Allele Type: Gene trapped
Allele
Name: RAD17 checkpoint clamp loader component; targeted mutation 1e, Helmholtz Zentrum Muenchen GmbH
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
Allele
Name: RAD17 checkpoint clamp loader component; targeted mutation 1e, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap EUCE307e04, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
Allele
Name: RAD17 checkpoint clamp loader component; targeted mutation 1a, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Conditional ready, Null/knockout, Reporter
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap AL0611, Wellcome Trust Sanger Institute
Allele Type: Gene trapped
Allele  
Name: RAD17 checkpoint clamp loader component; gene trap IST14431A11, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
Genotype
Symbol: Rad17/Rad17
Background: involves: 129P2/OlaHsd * C57BL/6
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Rad17/Rad17<+>
Background: involves: 129P2/OlaHsd * C57BL/6
Zygosity: ht
Has Mutant Allele: true
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
Publication
First Author: Aylon Y
Year: 2003
Journal: Mol Cell Biol
Title: The checkpoint protein Rad24 of Saccharomyces cerevisiae is involved in processing double-strand break ends and in recombination partner choice.
Volume: 23
Issue: 18
Pages: 6585-96
Publication
First Author: Yu S
Year: 2001
Journal: Mutat Res
Title: RAD9, RAD24, RAD16 and RAD26 are required for the inducible nucleotide excision repair of UV-induced cyclobutane pyrimidine dimers from the transcribed and non-transcribed regions of the Saccharomyces cerevisiae MFA2 gene.
Volume: 485
Issue: 3
Pages: 229-36
Publication
First Author: de la Torre-Ruiz M
Year: 2000
Journal: FEBS Lett
Title: The Saccharomyces cerevisiae DNA damage checkpoint is required for efficient repair of double strand breaks by non-homologous end joining.
Volume: 467
Issue: 2-3
Pages: 311-5
Publication
First Author: Zubko MK
Year: 2004
Journal: Genetics
Title: Exo1 and Rad24 differentially regulate generation of ssDNA at telomeres of Saccharomyces cerevisiae cdc13-1 mutants.
Volume: 168
Issue: 1
Pages: 103-15
Publication
First Author: Kataoka A
Year: 2001
Journal: Clin Cancer Res
Title: Overexpression of HRad17 mRNA in human breast cancer: correlation with lymph node metastasis.
Volume: 7
Issue: 9
Pages: 2815-20
Publication
First Author: Parker AE
Year: 1998
Journal: J Biol Chem
Title: A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease.
Volume: 273
Issue: 29
Pages: 18332-9
Protein Domain
Type: Family
Description: This entry represents checkpoint protein Rad24 from budding yeasts and its homologue, Rad17 from other organisms. In Saccharomyces cerevisiae, Rad24 forms a complex with replication factor C (RFC) proteins, including Rfc2, Rfc3, Rfc4, and Rfc5. When DNA damage is detected, the Rad24-RFC complex loads Rad17-Mec3-Ddc1 complex onto chromatin and activates DNA damage checkpoint, which then leads to cell cycle arrest and DNA repair []. The Rad24-RFC complex is involved in both the mitotic and meiotic checkpoints []. Besides checkpoint activation, Rad24 is also involved in double-strand break ends processing, DNA repair and telomere maintenance [, , , ]. In human, the comparable DNA damage checkpoint components, Rad17 and the Rad1-Rad9-Hus1 (9-1-1) complex, play similar roles in DNA damage surveillance and checkpoint activation as their counter partners (Rad24, Rad17-Mec3-Ddc1) in budding yeast. Rad17 participates in the recruitment of the 9-1-1 complex onto chromatin. Besides checkpoint activation, Rad17 may also serve as a sensor of DNA replication progression, and may be involved in homologous recombination []. Overexpression of Rad17 has been associated with human breast and colon cancers [, ]. It's worth noting that the name, Rad17, has been used for different proteins in budding yeast and other organisms. In this entry, Rad17, is the homologue of the budding yeast Rad24 and has no homology with budding yeast Rad17
Protein Domain
Type: Family
Description: This entry consists of the checkpoint protein Rad24 from budding yeast and its homologue, Rad17, from other organisms. This entry does not include Rad17 from plants. In Saccharomyces cerevisiae, Rad24 forms a complex with replication factor C (RFC) proteins, including Rfc2, Rfc3, Rfc4, and Rfc5. When DNA damage is detected, the Rad24-RFC complex loads Rad17-Mec3-Ddc1 complex onto chromatin and activates DNA damage checkpoint, which then leads to cell cycle arrest and DNA repair []. The Rad24-RFC complex is involved in both the mitotic and meiotic checkpoints []. Besides checkpoint activation, Rad24 is also involved in double-strand break ends processing, DNA repair and telomere maintenance [, , , ]. In human, the comparable DNA damage checkpoint components, Rad17 and the Rad1-Rad9-Hus1 (9-1-1) complex, play similar roles in DNA damage surveillance and checkpoint activation as their counter partners (Rad24, Rad17-Mec3-Ddc1) in budding yeast. Rad17 participates in the recruitment of the 9-1-1 complex onto chromatin. Besides checkpoint activation, Rad17 may also serve as a sensor of DNA replication progression, and may be involved in homologous recombination []. Overexpression of Rad17 has been associated with human breast and colon cancers [, ]. It's worth noting that the name, Rad17, has been used for different proteins in budding yeast and other organisms. In this entry, Rad17, is the homologue of the budding yeast Rad24 and has no homology with budding yeast Rad17
Protein
Organism: Mus musculus/domesticus
Length: 785  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 47  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 758  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 585  
Fragment?: false
Publication
First Author: Zou L
Year: 2003
Journal: Science
Title: Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes.
Volume: 300
Issue: 5625
Pages: 1542-8
Publication
First Author: Zhang H
Year: 2016
Journal: Cell Rep
Title: ATRIP Deacetylation by SIRT2 Drives ATR Checkpoint Activation by Promoting Binding to RPA-ssDNA.
Volume: 14
Issue: 6
Pages: 1435-1447
Protein Domain
Type: Family
Description: The function of the ATR-ATRIP (ATR-interacting protein) protein kinase complex is crucial for the cellular response to replication stress and DNA damage. ATRIP is a regulatory partner of ATR. The binding of ATRIP to replication protein A-coated ssDNA at sites of DNA damage drives ATR activation and enables the ATR-ATRIP complex to stimulate phosphorylation of substrates, such as Rad17 or Chk1, and the initiation of checkpoint signalling []. ATRIP deacetylation by SIRT2 promotes ATR-ATRIP bindingto RPA-ssDNA [].
Protein
Organism: Mus musculus/domesticus
Length: 688  
Fragment?: false
Publication
First Author: Li X
Year: 1999
Journal: Cell
Title: Identification and cloning of a negative regulator of systemic acquired resistance, SNI1, through a screen for suppressors of npr1-1.
Volume: 98
Issue: 3
Pages: 329-39
Publication
First Author: Kim HS
Year: 2012
Journal: Nucleic Acids Res
Title: A NAC transcription factor and SNI1 cooperatively suppress basal pathogen resistance in Arabidopsis thaliana.
Volume: 40
Issue: 18
Pages: 9182-92
Protein Domain
Type: Family
Description: SNI1 was isolated in a screen for negative regulators of NPR1, a transcriptional coactivator of plant pathogen defence gene PR1 []. SNl1 has been shown to cooperate with the transcription repressor CBNAC, which binds to cis-elements on the PR1 promoter, to suppress PR1 expression []. SNI1 also regulates DNA damage sensor proteins RAD17 and ATR, suggesting that DNA damage responses is an intrinsic component of the plant immune responses. SNI1 is a subunit of the Structural Maintenance of Chromosome (SMC) 5/6 complex involved in DNA damage responses [].
Protein Domain
Type: Family
Description: Rec1 of Ustilago maydis is a homologue of S. pombe Rad1 and S. cerevisiae Rad17 proteins. It plays a key role in regulating the genetic systemof the fungus. Rec1 mutants are very sensitive to UV light - mutationleads to a complex phenotype with alterations in DNA repair, recombination,mutagenesis, meiosis and cell division. The predicted product of theREC1 gene is a polypeptide of 522 amino acid residues with molecular mass 57 kD. The protein shows 3'--5' exonuclease activity, but only in cellsover-expressing Rec1. While it is distinguishable from the majorbacterial nucleases, the protein has certain enzymatic features in commonwith epsilon, the proof-reading exonuclease subunit of Escherichia coli DNA polymeraseIII holoenzyme [].
Publication
First Author: Freire R
Year: 1998
Journal: Genes Dev
Title: Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosis.
Volume: 12
Issue: 16
Pages: 2560-73
Publication
First Author: Dean FB
Year: 1998
Journal: Genomics
Title: cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster.
Volume: 54
Issue: 3
Pages: 424-36
Publication
First Author: Jiang K
Year: 2003
Journal: J Biol Chem
Title: Regulation of Chk1 includes chromatin association and 14-3-3 binding following phosphorylation on Ser-345.
Volume: 278
Issue: 27
Pages: 25207-17
Protein
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
Publication
First Author: Gartner A
Year: 2000
Journal: Mol Cell
Title: A conserved checkpoint pathway mediates DNA damage--induced apoptosis and cell cycle arrest in C. elegans.
Volume: 5
Issue: 3
Pages: 435-43
Publication
First Author: Ahmed S
Year: 2000
Journal: Nature
Title: MRT-2 checkpoint protein is required for germline immortality and telomere replication in C. elegans.
Volume: 403
Issue: 6766
Pages: 159-64
Publication
First Author: Harris J
Year: 2006
Journal: Genetics
Title: Mutator phenotype of Caenorhabditis elegans DNA damage checkpoint mutants.
Volume: 174
Issue: 2
Pages: 601-16
Publication
First Author: St Onge RP
Year: 1999
Journal: Mol Biol Cell
Title: The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1.
Volume: 10
Issue: 6
Pages: 1985-95
Publication
First Author: Hang H
Year: 2000
Journal: Genomics
Title: Physical interactions among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression.
Volume: 65
Issue: 1
Pages: 24-33
Publication
First Author: Majka J
Year: 2005
Journal: DNA Repair (Amst)
Title: Function of Rad17/Mec3/Ddc1 and its partial complexes in the DNA damage checkpoint.
Volume: 4
Issue: 10
Pages: 1189-94
Protein Domain
Type: Family
Description: This family consists of the repair proteins Rad1, Rec1 and Rad17.Rad1 is a component of the 9-1-1 cell-cycle checkpoint response complex (Rad9-Rad1-Hus1) that plays a major role in DNA repair [, ]. Rad1 isoform 1 possesses 3'->5' double stranded DNA exonuclease activity [].Rec1 of Ustilago maydis plays a key role in regulating the genetic system of this fungus. Rec1 mutants are very sensitive to UV light. Mutation leads to a complex phenotype with alterations in DNA repair, recombination, mutagenesis, meiosis and cell division []. Rec1 shows 3'--5' exonuclease activity, but only in cells over-expressing Rec1. Rad17 is a budding yeast checkpoint protein. It is a component of the checkpoint clamp complex (composed of Ddc1, Mec3 and Rad17) involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes [, , ]. The Ddc1-Mec3-Rad17 clamp complex shows no detectable exonuclease activity [].
Protein Domain
Type: Family
Description: This entry represents the budding yeast Ddc1, which is homologous to the fission yeast and human Rad9.DNA-damage checkpoint protein 1 (Ddc1) forms a checkpoint clamp complex with Mec3 and Rad17 [, ]. This complex plays a role in the surveillance system that permits DNA-repair pathways to restore the integrity of DNA in advance of DNA synthesis or separation of replicated chromosomes, thereby ensuring that new phases are not entered if DNA is damaged []. Ddc1 can activate Mec1 (the principal checkpoint protein kinase, human ATR homologue) in G1 phase. In G2 phase, Ddc1 can either activate Mec1 directly or recruit Dpb11 (ortholog of human TopBP1) and subsequently activate Mec1 []. Ddc1 does not have the DNA exonuclease function [].
Protein Domain
Type: Family
Description: Rad1 is a component of the 9-1-1 cell-cycle checkpoint response complex, which plays a role in checkpoint activation that permits DNA-repair pathways to prevent cell cycle progression in response to DNA damage and replication stress [, ]. The 9-1-1 complex is recruited to DNA lesions upon damage by the Rad17 (Rad24 in budding yeast)-replication factor C (RFC) clamp loader complex. The 9-1-1 complex is necessary for the recruitment of C12orf32/RHINO to sites of double-stranded breaks (DSB) occurring during the S phase []. Rad1 isoform 1 possesses 3'->5' double stranded DNA exonuclease activity [].In Caenorhabditis elegans, the cell cycle checkpoint protein RAD1 homologue mrt-2 has a role in genome stability by promoting DNA double strand break-induced cell cycle arrest and apoptosis, and is required for maintaining telomere length and germline immortality [, , ].
Protein
Organism: Mus musculus/domesticus
Length: 280  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: true
Publication
First Author: Thelen MP
Year: 1994
Journal: J Biol Chem
Title: The REC1 gene of Ustilago maydis involved in the cellular response to DNA damage encodes an exonuclease.
Volume: 269
Issue: 1
Pages: 747-54
Publication
First Author: Yan S
Year: 2013
Journal: Mol Cell
Title: Salicylic acid activates DNA damage responses to potentiate plant immunity.
Volume: 52
Issue: 4
Pages: 602-10
Publication
First Author: Longhese MP
Year: 1997
Journal: EMBO J
Title: The novel DNA damage checkpoint protein ddc1p is phosphorylated periodically during the cell cycle and in response to DNA damage in budding yeast.
Volume: 16
Issue: 17
Pages: 5216-26
Publication
First Author: Cotta-Ramusino C
Year: 2011
Journal: Science
Title: A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling.
Volume: 332
Issue: 6035
Pages: 1313-7
Publication
First Author: Navadgi-Patil VM
Year: 2009
Journal: Mol Cell
Title: The unstructured C-terminal tail of the 9-1-1 clamp subunit Ddc1 activates Mec1/ATR via two distinct mechanisms.
Volume: 36
Issue: 5
Pages: 743-53
Publication
First Author: Eichinger CS
Year: 2011
Journal: Trends Biochem Sci
Title: 9-1-1: PCNA's specialized cousin.
Volume: 36
Issue: 11
Pages: 563-8
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
Publication
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112