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Search results 201 to 276 out of 276 for Rad1

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Type Details Score
Publication
21659603 | -
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
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Allele
Rad1<Gt(D146C09)Wrst> | MGI:3892102
 
Name: RAD1 checkpoint DNA exonuclease; gene trap D146C09, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad1<Gt(E087F07)Wrst> | MGI:3895590
 
Name: RAD1 checkpoint DNA exonuclease; gene trap E087F07, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad1<Gt(E152B03)Wrst> | MGI:3909956
 
Name: RAD1 checkpoint DNA exonuclease; gene trap E152B03, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad1<Gt(E148A08)Wrst> | MGI:3915916
 
Name: RAD1 checkpoint DNA exonuclease; gene trap E148A08, German Gene Trap Consortium
Allele Type: Gene trapped
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Strain
MGI:6440050 | B6;129S5-Rad1<Gt(OST347989)Lex>/Tac
Attribute String: mutant stock, gene trap
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Allele
Rad1<Gt(AE0751)Wtsi> | MGI:4338124
 
Name: RAD1 checkpoint DNA exonuclease; gene trap AE0751, Wellcome Trust Sanger Institute
Allele Type: Gene trapped
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Allele
Rad1<tm1a(KOMP)Wtsi> | MGI:4364310
Name: RAD1 checkpoint DNA exonuclease; targeted mutation 1a, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Conditional ready, Null/knockout, Reporter
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Allele
Rad1<Gt(EUCE0295a05)Hmgu> | MGI:4368693
 
Name: RAD1 checkpoint DNA exonuclease; gene trap EUCE0295a05, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
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Allele
Rad1<Gt(EUCE0185g02)Hmgu> | MGI:4369836
 
Name: RAD1 checkpoint DNA exonuclease; gene trap EUCE0185g02, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
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Allele
Rad1<Gt(EUCE0163e01)Hmgu> | MGI:4372412
 
Name: RAD1 checkpoint DNA exonuclease; gene trap EUCE0163e01, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
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Allele
Rad1<Gt(EUCE0299c11)Hmgu> | MGI:4375221
 
Name: RAD1 checkpoint DNA exonuclease; gene trap EUCE0299c11, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
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Allele
Rad1<Gt(EUCE0092h10)Hmgu> | MGI:4390003
 
Name: RAD1 checkpoint DNA exonuclease; gene trap EUCE0092h10, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
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Allele
Rad1<Gt(EUCE322b03)Hmgu> | MGI:4397304
 
Name: RAD1 checkpoint DNA exonuclease; gene trap EUCE322b03, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
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Allele
Rad1<tm1a(KOMP)Mbp> | MGI:4843782
Name: RAD1 checkpoint DNA exonuclease; targeted mutation 1a, Mouse Biology Program, UC Davis
Allele Type: Targeted
Attribute String: Conditional ready, Null/knockout, Reporter
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Allele
Rad1<tm1e(KOMP)Mbp> | MGI:4843819
Name: RAD1 checkpoint DNA exonuclease; targeted mutation 1e, Mouse Biology Program, UC Davis
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Allele
Rad1<Gt(426F8)Cmhd> | MGI:4961522
 
Name: RAD1 checkpoint DNA exonuclease; gene trap 426F8, Centre for Modeling Human Disease
Allele Type: Gene trapped
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Allele
Rad1<Gt(101B3)Cmhd> | MGI:4971989
 
Name: RAD1 checkpoint DNA exonuclease; gene trap 101B3, Centre for Modeling Human Disease
Allele Type: Gene trapped
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Allele
Rad1<Gt(IST13210D4)Tigm> | MGI:5156269
 
Name: RAD1 checkpoint DNA exonuclease; gene trap IST13210D4, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad1<Gt(IST13391B1)Tigm> | MGI:5170830
 
Name: RAD1 checkpoint DNA exonuclease; gene trap IST13391B1, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad1<Gt(IST13863A9)Tigm> | MGI:5197926
 
Name: RAD1 checkpoint DNA exonuclease; gene trap IST13863A9, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad1<Gt(IST13872B8)Tigm> | MGI:5198482
 
Name: RAD1 checkpoint DNA exonuclease; gene trap IST13872B8, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad1<Gt(IST14013B5)Tigm> | MGI:5205436
 
Name: RAD1 checkpoint DNA exonuclease; gene trap IST14013B5, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad1<Gt(IST14255B12)Tigm> | MGI:5217857
 
Name: RAD1 checkpoint DNA exonuclease; gene trap IST14255B12, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad1<Gt(IST14386A4)Tigm> | MGI:5229080
 
Name: RAD1 checkpoint DNA exonuclease; gene trap IST14386A4, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad1<Gt(IST14507F2)Tigm> | MGI:5240322
 
Name: RAD1 checkpoint DNA exonuclease; gene trap IST14507F2, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad1<Gt(IST14580D8)Tigm> | MGI:5242410
 
Name: RAD1 checkpoint DNA exonuclease; gene trap IST14580D8, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad1<tm1b(KOMP)Wtsi> | MGI:5605756
Name: RAD1 checkpoint DNA exonuclease; targeted mutation 1b, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Strain
MGI:7577076 | C57BL/6JGpt-Rad1<em1Gpt>/Gpt
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Genotype
Genotype
Symbol: Rad1/Rad1
Background: involves: 129P2/OlaHsd * 129S4/SvJaeSor
Zygosity: hm
Has Mutant Allele: true
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Strain
MGI:5603831 | C57BL/6N-Rad1<tm1a(KOMP)Wtsi>/J
Attribute String: mutant strain, targeted mutation
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Strain
MGI:6347081 | C57BL/6N-Rad1<tm1a(KOMP)Wtsi>/JMmucd
Attribute String: mutant strain, coisogenic, targeted mutation
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Strain
MGI:5767518 | C57BL/6N-Rad1<tm1b(KOMP)Wtsi>/J
Attribute String: coisogenic, targeted mutation
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Strain
MGI:5608778 | B6N(Cg)-Rad1<tm1b(KOMP)Wtsi>/J
Attribute String: targeted mutation, mutant strain
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Strain
MGI:6347082 | C57BL/6N-Rad1<tm1b(KOMP)Wtsi>/JMmucd
Attribute String: mutant strain, coisogenic, targeted mutation
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Genotype
Genotype
Symbol: Rad1/Rad1
Background: C57BL/6N-Rad1/J
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Rad1/Rad1<+>
Background: C57BL/6N-Rad1/J
Zygosity: ht
Has Mutant Allele: true
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Protein Domain
IPR006167 | XPF
Type: Family
Description: This entry includes XPF from animals, Rad1 from budding yeasts and Rad16 from fission yeasts. Human XPF is a catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. It is involved in homologous recombination that assists in removing interstrand cross-link []. Budding yeast Rad1 and Rad10 form an endonuclease that specifically degrades single-stranded DNA [].
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Publication
19596235 | -
First Author: Svendsen JM
Year: 2009
Journal: Cell
Title: Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair.
Volume: 138
Issue: 1
Pages: 63-77
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Publication
35133274 | J:326477
   
First Author: Pereira C
Year: 2022
Journal: Elife
Title: Multiple 9-1-1 complexes promote homolog synapsis, DSB repair, and ATR signaling during mammalian meiosis.
Volume: 11
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Protein Domain
IPR003027 | Rec1_exonuc_Ustilaginaceae
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 [].
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Publication
10359610 | -
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
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Publication
10777662 | -
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
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Publication
16137930 | -
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
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Protein Domain
IPR003021 | Rad1_Rec1_Rad17
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 [].
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Publication
8276878 | -
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
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Publication
19918068 | J:155573
First Author: Yazinski SA
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Dual inactivation of Hus1 and p53 in the mouse mammary gland results in accumulation of damaged cells and impaired tissue regeneration.
Volume: 106
Issue: 50
Pages: 21282-7
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Publication
10382071 | J:55411
First Author: Moens PB
Year: 1999
Journal: Chromosoma
Title: The association of ATR protein with mouse meiotic chromosome cores.
Volume: 108
Issue: 2
Pages: 95-102
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Publication
7859947 | J:22679
First Author: Doria A
Year: 1995
Journal: Diabetes
Title: Trinucleotide repeats at the rad locus. Allele distributions in NIDDM and mapping to a 3-cM region on chromosome 16q.
Volume: 44
Issue: 2
Pages: 243-7
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Protein
F6VRS2
Organism: Mus musculus/domesticus
Length: 92  
Fragment?: true
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Protein
A0A494BAY5
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
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Protein
A0A494BAL0
Organism: Mus musculus/domesticus
Length: 73  
Fragment?: false
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Protein
D3Z515
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
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Protein
A0A494B9R8
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: true
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Protein
Q8QZZ4
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: true
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Publication
17720715 | -
First Author: Tripsianes K
Year: 2007
Journal: Nucleic Acids Res
Title: Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization.
Volume: 35
Issue: 17
Pages: 5789-98
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Publication
16428464 | -
First Author: Guzder SN
Year: 2006
Journal: Mol Cell Biol
Title: Complex formation with damage recognition protein Rad14 is essential for Saccharomyces cerevisiae Rad1-Rad10 nuclease to perform its function in nucleotide excision repair in vivo.
Volume: 26
Issue: 3
Pages: 1135-41
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Protein Domain
IPR004579 | ERCC1/RAD10/SWI10
Type: Family
Description: This family includes Rad10 from budding yeasts, Swi10 from fission yeasts and ERCC-1 from animals andplants. All proteins in this family for which functions are known are components in a multiprotein endonuclease complex (usually made up of Rad1 and Rad10 homologues). This complex is used primarily for nucleotide excision repair but also for some aspects of recombination repair. In budding yeast, Rad10 works as a heterodimer with Rad1, and is involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts or cross-linking agents. The complex forms an endonuclease which specifically degrades single-stranded DNA [].ERCC1 and XPF (xeroderma pigmentosum group F-complementing protein) are two structure-specific endonucleases of a class of seven containing an ERCC4 domain. Together they form an obligate complex that functions primarily in nucleotide excision repair (NER), a versatile pathway able to detect and remove a variety of DNA lesions induced by UV light and environmental carcinogens, and secondarily in DNA inter-strand cross-link repair and telomere maintenance. This domain in fact binds simultaneously to both XPF and single-stranded DNA; this ternary complex explains the important role of Ercc1 in targeting its catalytic XPF partner to the NER pre-incision complex [].
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Protein Domain
IPR007268 | Rad9/Ddc1
Type: Family
Description: This entry represents the DNA damage checkpoint protein Rad9 and its homologue in budding yeast, Ddc1. Rad9 forms a complex with Hus1 and Rad1 (called 9-1-1 complex). Ddc1 forms a similar complex with Mec1 and Rad17. Structurally, the 9-1-1 / Ddc1-Mec3-Rad17 complex is similar to the PCNA complex, which forms trimeric ring-shaped clamps. The 9-1-1 / Ddc1-Mec3-Rad17 complex plays a role in checkpoint activation that permits DNA-repair pathways to prevent cell cycle progression in response to DNA damage and replication stress [, ].In humans, 9-1-1 binds to TopBP1 and activates the ATR-Chk1 checkpoint pathway []. Besides its function in the 9-1-1 complex, Rad9 can also act as a transcriptional factor and participate in immunoglobulin class switch recombination []. It also shows 3'-5' exonuclease activity []. Aberrant Rad9 expression has been associated with prostate, breast, lung, skin, thyroid, and gastric cancers [].In budding yeast, 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 (the orthologue of human TopBP1) and subsequently activate Mec1 []. Ddc1 does not have DNA exonuclease function [].It is worth noting that the Rad9 proteins referred to in this entry are the mammalian and fission yeast homologues of budding yeast Ddc1. Members of this family do not share the sequence homology another DNA damage-dependent checkpoint protein from budding yeast, confusingly also called Rad9.
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Protein
Q9QZD4
Organism: Mus musculus/domesticus
Length: 917  
Fragment?: false
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Publication
8649984 | -
First Author: Siede W
Year: 1996
Journal: Nucleic Acids Res
Title: Cloning and characterization of RAD17, a gene controlling cell cycle responses to DNA damage in Saccharomyces cerevisiae.
Volume: 24
Issue: 9
Pages: 1669-75
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Protein
Q9Z0F6
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
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Protein
Q6WBX7
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
Q8VC54
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
D3Z3W7
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: false
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Publication
22034047 | -
First Author: Broustas CG
Year: 2012
Journal: J Cell Biochem
Title: Contributions of Rad9 to tumorigenesis.
Volume: 113
Issue: 3
Pages: 742-51
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Publication
20005839 | -
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
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Publication
22925454 | -
First Author: Ueda S
Year: 2012
Journal: Genes Cells
Title: Two serine phosphorylation sites in the C-terminus of Rad9 are critical for 9-1-1 binding to TopBP1 and activation of the DNA damage checkpoint response in HeLa cells.
Volume: 17
Issue: 10
Pages: 807-16
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Publication
10713044 | -
First Author: Bessho T
Year: 2000
Journal: J Biol Chem
Title: Human DNA damage checkpoint protein hRAD9 is a 3' to 5' exonuclease.
Volume: 275
Issue: 11
Pages: 7451-4
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Publication
20729201 | J:166880
First Author: An L
Year: 2010
Journal: J Biol Chem
Title: Rad9 is required for B cell proliferation and immunoglobulin class switch recombination.
Volume: 285
Issue: 46
Pages: 35267-73
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Protein
H3BLF5
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: true
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Protein
E9PUM0
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Publication
12604797 | -
First Author: Majka J
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint.
Volume: 100
Issue: 5
Pages: 2249-54
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Protein
P07903
Organism: Mus musculus/domesticus
Length: 298  
Fragment?: false
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Publication
15489334 | -
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
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Publication
19468303 | -
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
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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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