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Search results 1001 to 1100 out of 1306 for Rad51

0.037s

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Type Details Score
Genotype
Symbol: Rad51c/Rad51c Krt14/Krt14<+>
Background: involves: 129P2/OlaHsd * 129S1/Sv * C57BL/6J
Zygosity: cn
Has Mutant Allele: true
Genotype
Symbol: Rad51c/Rad51c Trp53/Trp53
Background: involves: 129P2/OlaHsd * 129S1/Sv * C57BL/6J
Zygosity: cx
Has Mutant Allele: true
Publication
First Author: Rajesh C
Year: 2011
Journal: Nucleic Acids Res
Title: The splicing-factor related protein SFPQ/PSF interacts with RAD51D and is necessary for homology-directed repair and sister chromatid cohesion.
Volume: 39
Issue: 1
Pages: 132-45
Genotype
Symbol: Rad51/Rad51 Ndor1/Ndor1<+>
Background: involves: 129S/Sv * C57BL/6J
Zygosity: cn
Has Mutant Allele: true
Genotype
Symbol: Rad51/Rad51 Speer6-ps1/Speer6-ps1
Background: involves: C57BL/6J
Zygosity: cn
Has Mutant Allele: true
Allele
Name: breast cancer 2, early onset; targeted mutation 1, Paul Hasty
Allele Type: Targeted
Attribute String: Hypomorph
Allele
Name: BRCA1 associated RING domain 1; targeted mutation 8.1, Richard J Baer
Allele Type: Targeted
Attribute String: Humanized sequence
Publication  
First Author: Gruver AM
Year: 2009
Journal: BMC Mol Biol
Title: Functional characterization and identification of mouse Rad51d splice variants.
Volume: 10
Pages: 27
Genotype
Symbol: Brca2/Brca2
Background: involves: 129S7/SvEvBrd * C57BL/6
Zygosity: hm
Has Mutant Allele: true
Protein
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
Publication
First Author: DiRuggiero J
Year: 1999
Journal: J Mol Evol
Title: DNA repair systems in archaea: mementos from the last universal common ancestor?
Volume: 49
Issue: 4
Pages: 474-84
Publication
First Author: Gasior SL
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: Assembly of RecA-like recombinases: distinct roles for mediator proteins in mitosis and meiosis.
Volume: 98
Issue: 15
Pages: 8411-8
Publication
First Author: Shinohara A
Year: 1999
Journal: Mutat Res
Title: Rad51/RecA protein families and the associated proteins in eukaryotes.
Volume: 435
Issue: 1
Pages: 13-21
Protein Domain
Type: Repeat
Description: The breast cancer type 2 susceptibility protein has a number of 39 amino acid repeats []that are critical for binding to RAD51 (a key protein in DNA recombinational repair) and resistance to methyl methanesulphonate treatment [, , ]. BRCA2 is a breast tumour suppressor with a potential function in the cellular response to DNA damage. At the cellular level, expressionis regulated in a cell-cycle dependent manner and peak expression of BRCA2 mRNA is found in S phase, suggesting BRCA2 may participate in regulating cell proliferation. There are eight repeats in BRCA2 designated as BRC1 to BRC8. BRC1, BRC2, BRC3, BRC4, BRC7, and BRC8 are highly conserved and bind to Rad51, whereas BRC5 and BRC6 are less well conserved and do not bind to Rad51 []. It has been suggested that BRCA2 plays a role in positioning Rad51 at the site of DNA repair or in removing Rad51 from DNA once repair has been completed.
Protein Domain
Type: Family
Description: RADX is an RPA-like, single-strand DNA binding proteinrecruited to replication forks to maintain genome stability []. It has been shown to modulate stalled fork protection by antagonizing RAD51 [].
Protein Domain
Type: Domain
Description: This domain is found at the C terminus of the DNA repair and recombination protein Rad51 and some Rad51-like proteins. It is critical for DNA binding []. Rad51 is a homologue of the bacterial RecA protein. Rad51 and RecA share a core ATPase domain.Rad51-like genes form two separate groups (RAD-alpha and RAD-beta), each of which contains both archaeal and eukaryotic members []. This group of recombinases includes the eukaryotic proteins Rad51, Rad57, the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group []. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as Rad55/57 [, ].
Publication
First Author: Lim PX
Year: 2024
Journal: Mol Cell
Title: BRCA2 promotes genomic integrity and therapy resistance primarily through its role in homology-directed repair.
Volume: 84
Issue: 3
Pages: 447-462.e10
Protein Domain
Type: Family
Description: DNA repair protein XRCC2 is a RAD51 paralogue. In humans, it is part of the protein complex BCDX2 (contains RAD51B, RAD51C, RAD51D, and XRCC2), which acts in the BRCA1-BRCA2-dependent homologous recombination pathway [, ]. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA []. Interestingly, XRCC2 and other homologous recombination proteins are associated with centrosomes and are required for mitotic stability [].
Genotype
Symbol: Rad51c/Rad51c Trp53/Trp53 Krt14/Krt14<+>
Background: involves: 129P2/OlaHsd * 129S1/Sv * C57BL/6J
Zygosity: cn
Has Mutant Allele: true
Publication
First Author: Lin Z
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Origins and evolution of the recA/RAD51 gene family: evidence for ancient gene duplication and endosymbiotic gene transfer.
Volume: 103
Issue: 27
Pages: 10328-33
Publication
First Author: Zeng F
Year: 2004
Journal: Dev Biol
Title: Transcript profiling during preimplantation mouse development.
Volume: 272
Issue: 2
Pages: 483-96
Publication
First Author: Bork P
Year: 1996
Journal: Nat Genet
Title: Internal repeats in the BRCA2 protein sequence.
Volume: 13
Issue: 1
Pages: 22-3
Publication
First Author: Marmorstein LY
Year: 1998
Journal: Proc Natl Acad Sci U S A
Title: The BRCA2 gene product functionally interacts with p53 and RAD51.
Volume: 95
Issue: 23
Pages: 13869-74
Publication
First Author: Chen CF
Year: 1999
Journal: J Biol Chem
Title: Expression of BRC repeats in breast cancer cells disrupts the BRCA2-Rad51 complex and leads to radiation hypersensitivity and loss of G(2)/M checkpoint control.
Volume: 274
Issue: 46
Pages: 32931-5
Publication
First Author: Donoho G
Year: 2003
Journal: Genes Chromosomes Cancer
Title: Deletion of Brca2 exon 27 causes hypersensitivity to DNA crosslinks, chromosomal instability, and reduced life span in mice.
Volume: 36
Issue: 4
Pages: 317-31
Publication
First Author: Morimatsu M
Year: 1998
Journal: Cancer Res
Title: Cells deleted for Brca2 COOH terminus exhibit hypersensitivity to gamma-radiation and premature senescence.
Volume: 58
Issue: 15
Pages: 3441-7
Strain
Attribute String: mutant stock, targeted mutation
Genotype
Symbol: Brca2/Brca2
Background: involves: 129S7/SvEvBrd * C57BL/6
Zygosity: ht
Has Mutant Allele: true
Publication
First Author: Catlett MG
Year: 2003
Journal: Mol Biol Cell
Title: Schizosaccharomyces pombe Rdh54 (TID1) acts with Rhp54 (RAD54) to repair meiotic double-strand breaks.
Volume: 14
Issue: 11
Pages: 4707-20
Publication
First Author: Solinger JA
Year: 2002
Journal: Mol Cell
Title: Rad54, a Swi2/Snf2-like recombinational repair protein, disassembles Rad51:dsDNA filaments.
Volume: 10
Issue: 5
Pages: 1175-88
Protein Domain
Type: Domain
Description: This domain is found at the C terminus of DNA repair and recombination protein Rad51, and eukaryotic and archaeal Rad51-like proteins. It is critical for DNA binding []. Rad51 is a homologue of the bacterial RecA protein. Rad51 and RecA share a core ATPase domain.Unlike eubacteria, several archaeal species have two recA/RAD51-like genes, called RadA and RadB. Among eukaryotes, yeast contain four RAD51-like genes (RAD51, DMC1, RAD55/rhp55, and RAD57/rhp57). In vertebrate animals and plants, there are different RAD51-like genes: RAD51, RAD51B, RAD51C, RAD51D, DMC1, XRCC2, and XRCC3 [].
Protein Domain
Type: Domain
Description: This is the N-terminal of the DNA repair protein Rad54 []. Rad54 functions in the recombinational DNA repair (RAD52) pathway. It dissociates RAD51 from nucleoprotein filaments formed on dsDNA and could be involved in the turnover of RAD51 protein-dsDNA filaments. Deficient mice also show significantly shorter telomeres than wild-type controls, indicating that the protein activity plays an essential role in telomere length maintenance in mammals. Non-homologous end joining (NHEJ) and homologous recombination (HR) represent the two major pathways of DNA double-strand break (DSB) repair in eukaryotic cells. LIG4 and RAD54L cooperate to support cellular proliferation, repair spontaneous DSBs, and prevent chromosome and single chromatid aberrations [, ].
Protein
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
Publication
First Author: Bonin I
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: Structural basis for the interaction of Escherichia coli NusA with protein N of phage lambda.
Volume: 101
Issue: 38
Pages: 13762-7
Publication
First Author: Eisenmann A
Year: 2005
Journal: Protein Sci
Title: The E. coli NusA carboxy-terminal domains are structurally similar and show specific RNAP- and lambdaN interaction.
Volume: 14
Issue: 8
Pages: 2018-29
Protein Domain
Type: Homologous_superfamily
Description: This superfamily represents an α-helical bundle domain, which has a SAM domain-like fold. This compact domain consists of a 4-5 helical bundle of two orthogonally packed alpha-hairpins, and contains one classic and one pseudo HhH (helix-hairpin-helix) motif. This domain is found at N-terminal of the DNA repair protein Rad51, at the C-terminal of the transcription elongation protein NusA, and at the C-terminal of the hypothetical protein AF1548.Human Rad51 protein is a homologue of Escherichia coli RecA protein, and functions in DNA repair and recombination []. In higher eukaryotes, Rad51 protein is essential for cell viability. The N-terminal region of Rad51 is highly conserved among eukaryotic Rad51 proteins but is absent from RecA, suggesting a Rad51-specific function for this region. The-terminal domain is involved in interactions with DNA and proteins; DNA binding may be regulated via phosphorylation within the N-terminal domain.NusA (N utilisation substance A) from E. coli is an essential transcription factor that associates with the RNA polymerase (RNAP) core enzyme, where it modulates transcriptional pausing, termination and anti-termination []. The C-terminal of NusA consists of two repeat units, and is responsible for the interaction of NisA with the C-terminal of RNAP, and with its interaction with protein N from phage lambda during anti-termination [].
Protein Domain
Type: Family
Description: Methyl methanesulfonate-sensitivity protein 22-like (MMS22L) is a component of the MMS22L-TONSL complex, a complex that stimulates the recombination-dependent repair of stalled or collapsed replication forks []. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication by promoting homologous recombination-mediated repair of replication fork-associated double-strand breaks [, ]. It may act by mediating the assembly of RAD51 filaments on ssDNA [].
Protein
Organism: Mus musculus/domesticus
Length: 992  
Fragment?: true
Publication
First Author: Seeliger K
Year: 2012
Journal: New Phytol
Title: BRCA2 is a mediator of RAD51- and DMC1-facilitated homologous recombination in Arabidopsis thaliana.
Volume: 193
Issue: 2
Pages: 364-75
Protein Domain
Type: Family
Description: The breast cancer type 2 susceptibility protein (BRCA2) is a breast tumour suppressor involved in double-strand break repair and/or homologous recombination []. BRCA2 gene expression is regulated in a cell-cycle dependent manner and peak expression of BRCA2 mRNA occurring in S phase, suggesting BRCA2 may participate in regulating cell proliferation. BRCA2, and related protein BRCA1, have transcriptional activation potential and the two proteins are associated with the activation of double-strand break repair and/or homologous recombination. The two proteins have been shown to coexist and colocalize in a biochemical complex. BRCA2 has a number of 39 amino acid repeats []that are critical for binding to RAD51 (a key protein in DNA recombinational repair) and resistance to methyl methanesulphonate treatment [, , ]. There are eight repeats in BRCA2 designated as BRC1 to BRC8. BRC1, BRC2, BRC3, BRC4, BRC7, and BRC8 have high sequence identity and bind to Rad51, whereas BRC5 and BRC6 are less well conserved and are unable to bind Rad51 []. It has been suggested that BRCA2 plays a role in positioning Rad51 at the site of DNA repair or in removing Rad51 from DNA once repair has been completed.Mutations in BRCA1 and BRCA2 have been linked to an elevated risk of young onset breast cancer and confer a high risk of the disease through a dominantly inherited fashion []. BRCA2 mutations are typically microdeletions.Homologues exist in plants: the BRCA2A and BRCA2B proteins from Arabidopsis thalianaare required for repair of breaks in double-stranded DNA and homologous recombination and in the prophase stage of meiosis are required for formation of RAD51 and DMC1 foci in males [].
Publication
First Author: Dickinson K
Year: 2023
Journal: Am J Physiol Renal Physiol
Title: WT1 regulates expression of DNA repair gene Neil3 during nephrogenesis.
Volume: 324
Issue: 3
Pages: F245-F255
Publication
First Author: Venkitaraman AR
Year: 2001
Journal: Curr Opin Cell Biol
Title: Chromosome stability, DNA recombination and the BRCA2 tumour suppressor.
Volume: 13
Issue: 3
Pages: 338-43
Publication
First Author: Titus S
Year: 2013
Journal: Sci Transl Med
Title: Impairment of BRCA1-related DNA double-strand break repair leads to ovarian aging in mice and humans.
Volume: 5
Issue: 172
Pages: 172ra21
Protein
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: true
Publication
First Author: Hayase A
Year: 2004
Journal: Cell
Title: A protein complex containing Mei5 and Sae3 promotes the assembly of the meiosis-specific RecA homolog Dmc1.
Volume: 119
Issue: 7
Pages: 927-40
Publication
First Author: Tao Y
Year: 2012
Journal: J Biol Chem
Title: Structural analysis of Shu proteins reveals a DNA binding role essential for resisting damage.
Volume: 287
Issue: 24
Pages: 20231-9
Publication
First Author: She Z
Year: 2012
Journal: FEBS Lett
Title: Structural and SAXS analysis of the budding yeast SHU-complex proteins.
Volume: 586
Issue: 16
Pages: 2306-12
Publication
First Author: Ball LG
Year: 2009
Journal: Mol Microbiol
Title: The yeast Shu complex couples error-free post-replication repair to homologous recombination.
Volume: 73
Issue: 1
Pages: 89-102
Protein Domain
Type: Family
Description: This entry includes Mei5 from budding yeasts and SFR1 from animals and fission yeasts. Although the fission yeast Swi5-Sfr1 complex is critical for homologous recombination repair, the budding yeast counterpart Sae3-Mei5 complex is meiosis-specific, interacts with Dmc1, and promotes assembly of Dmc1 on meiotic chromosomes [].SFR is a component of the SWI5-SFR1 complex, a complex required for double-strand break repair via homologous recombination []. Mei5 is one of a pair of meiosis-specific proteins which facilitate the loading of Dmc1 on to Rad51 on DNA at double-strand breaks during recombination. Recombination is carried out by a large protein complex based around the two RecA homologues, Rad51 and Dmc1 []. This complex may play both a catalytic and a structural role in the interaction between homologous chromosomes during meiosis. Mei5 is seen to contain a coiled-coli region.
Protein
Organism: Mus musculus/domesticus
Length: 600  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 106  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 605  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: true
Publication
First Author: McIlwraith MJ
Year: 2001
Journal: Nucleic Acids Res
Title: RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination.
Volume: 29
Issue: 22
Pages: 4509-17
Publication
First Author: Gauci S
Year: 2009
Journal: Anal Chem
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Volume: 81
Issue: 11
Pages: 4493-501
Protein Domain
Type: Family
Description: Brme1 (also known as Meiok21) is a component of meiotic recombination bridges involved in meiotic double-strand break repair [, ]. The C-terminal domain of Brme1 physically interacts with the N-terminal domain of HSF2BP []. BRME1 facilitates the loading of RAD51 and DMC1 recombinases onto DSBs (DNA double-strand breaks) through interaction with MEILB2/HSF2BP and replacing ssDNA binding proteins []. Brme1 is highly expressed in mice testes and fetal ovaries. Knockout of Brme1 results in male mice infertility [].
Protein Domain
Type: Family
Description: Csm2 (chromosome segregation in meiosis protein 2) is a component of the Shu complex (also known as PCSS complex) involved in the error-free DNA post-replication repair (PRR) []. Psy3 forms a complex first with Cms2, and their L2 loops confer the DNA-binding activity to the Shu complex [, ]. The Shu complex binds to recombination sites and is required for Rad51 assembly and function during meiosis. Psy3-Csm2 constitutes a core sub-complex that can stabilise the Rad51-single-stranded DNA complex independently of nucleotide cofactor [].
Protein Domain
Type: Family
Description: Psy3 is a component of the Shu complex (also known as PCSS complex) involved in the error-free DNA post-replication repair (PRR) []. Psy3 forms a complex first with Cms2, and their L2 loops confer the DNA-binding activity to the Shu complex [, ]. The Shu complex binds to recombination sites and is required for Rad51 assembly and function during meiosis. Psy3-Csm2 constitutes a core sub-complex that can stabilise the Rad51-single-stranded DNA complex independently of nucleotide cofactor [].
Protein Domain
Type: Family
Description: This family consists exclusively of archaeal RadA protein, a homologue of bacterial RecA, eukaryotic RAD51 (), and archaeal RadB (). This protein is involved in DNA repair and in homologous recombination, it binds and assembles on single-stranded DNA to form a nucleoprotein filament. RadA hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules involved in DNA repair and recombination. The member from Pyrococcus horikoshii contains an intein [].
Protein Domain
Type: Family
Description: RAD51-associated protein 1 may participate in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair []. It functionally cooperates with PALB2 in promoting of D-loop formation by RAD51 [, ]. It binds to single and double stranded DNA, and is capable of aggregating DNA []. It also binds RNA []. It is phosphorylated upon DNA damage, probably by ATM or ATR [, , ].
Protein Domain
Type: Domain
Description: This entry represents the C-terminal of the MMS22L (Methyl methanesulfonate-sensitivity protein 22-like) protein. MMS22L is a component of the MMS22L-TONSL complex, a complex that stimulates the recombination-dependent repair of stalled or collapsed replication forks []. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication by promoting homologous recombination-mediated repair of replication fork-associated double-strand breaks [, ]. It may act by mediating the assembly of RAD51 filaments on ssDNA [].
Protein Domain
Type: Domain
Description: This entry represents the N-terminal of the MMS22L (Methyl methanesulfonate-sensitivity protein 22-like) protein.Methyl methanesulfonate-sensitivity protein 22-like (MMS22L) is a component of the MMS22L-TONSL complex, a complex that stimulates the recombination-dependent repair of stalled or collapsed replication forks []. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication by promoting homologous recombination-mediated repair of replication fork-associated double-strand breaks [, ]. It may act by mediating the assembly of RAD51 filaments on ssDNA [].
Protein
Organism: Mus musculus/domesticus
Length: 1238  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1198  
Fragment?: false
Publication
First Author: O'Donnell L
Year: 2010
Journal: Mol Cell
Title: The MMS22L-TONSL complex mediates recovery from replication stress and homologous recombination.
Volume: 40
Issue: 4
Pages: 619-31
Publication
First Author: Duro E
Year: 2010
Journal: Mol Cell
Title: Identification of the MMS22L-TONSL complex that promotes homologous recombination.
Volume: 40
Issue: 4
Pages: 632-44
Publication
First Author: O'Connell BC
Year: 2010
Journal: Mol Cell
Title: A genome-wide camptothecin sensitivity screen identifies a mammalian MMS22L-NFKBIL2 complex required for genomic stability.
Volume: 40
Issue: 4
Pages: 645-57
HT Experiment  
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
Publication
First Author: Le Bras S
Year: 2002
Journal: Gene
Title: Transcript map of the Ovum mutant (Om) locus: isolation by exon trapping of new candidate genes for the DDK syndrome.
Volume: 296
Issue: 1-2
Pages: 75-86
Protein
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
Publication
First Author: Blundred R
Year: 2010
Journal: DNA Repair (Amst)
Title: Human RECQL5 overcomes thymidine-induced replication stress.
Volume: 9
Issue: 9
Pages: 964-75
Publication
First Author: Islam MN
Year: 2010
Journal: Mol Cell Biol
Title: RecQL5 promotes genome stabilization through two parallel mechanisms--interacting with RNA polymerase II and acting as a helicase.
Volume: 30
Issue: 10
Pages: 2460-72
Publication
First Author: Kassube SA
Year: 2013
Journal: Nat Struct Mol Biol
Title: Structural mimicry in transcription regulation of human RNA polymerase II by the DNA helicase RECQL5.
Volume: 20
Issue: 7
Pages: 892-9
Publication
First Author: Ramamoorthy M
Year: 2013
Journal: Carcinogenesis
Title: The RecQ helicase RECQL5 participates in psoralen-induced interstrand cross-link repair.
Volume: 34
Issue: 10
Pages: 2218-30
Publication
First Author: Ramamoorthy M
Year: 2012
Journal: Nucleic Acids Res
Title: RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation and cell cycle progression.
Volume: 40
Issue: 4
Pages: 1621-35
Publication
First Author: Liu S
Year: 2011
Journal: J Biol Chem
Title: RING finger and WD repeat domain 3 (RFWD3) associates with replication protein A (RPA) and facilitates RPA-mediated DNA damage response.
Volume: 286
Issue: 25
Pages: 22314-22
Publication
First Author: Gong Z
Year: 2011
Journal: J Biol Chem
Title: E3 ligase RFWD3 participates in replication checkpoint control.
Volume: 286
Issue: 25
Pages: 22308-13
Publication
First Author: Elia AE
Year: 2015
Journal: Mol Cell
Title: RFWD3-Dependent Ubiquitination of RPA Regulates Repair at Stalled Replication Forks.
Volume: 60
Issue: 2
Pages: 280-93
Publication
First Author: Sy SM
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: PALB2 is an integral component of the BRCA complex required for homologous recombination repair.
Volume: 106
Issue: 17
Pages: 7155-60
Publication
First Author: Hartford SA
Year: 2016
Journal: PLoS Genet
Title: Interaction with PALB2 Is Essential for Maintenance of Genomic Integrity by BRCA2.
Volume: 12
Issue: 8
Pages: e1006236
Publication
First Author: Ducy M
Year: 2019
Journal: Trends Biochem Sci
Title: The Tumor Suppressor PALB2: Inside Out.
Volume: 44
Issue: 3
Pages: 226-240
Protein Domain
Type: Domain
Description: This entry represents a domain found in RECQ5. RecQ helicases is a group of highly conserved 3'-5' DNA helicases involved in maintaining genomic stability. RECQ5 plays an important role in DNA replication, transcription and repair [, ]. It interacts with RNA polymerase II to reduce transcription-associated replication impairment and recombination []. As a helicase, it can disrupt RAD51 filaments assembled on ssDNA, thereby inhibiting homologous recombination []. It also participates in psoralen-induced interstrand cross-link repair []. It stimulates DNA decatenation mediated by TOP2A [].
Protein Domain
Type: Family
Description: PALB2 (partner and Localizer of BRCA2) binds to the N-terminal region of BRCA2, and is vital for its function by facilitating its subnuclear localization []. It binds BRCA1 and BRCA2 and serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex, which is required for homologous recombination repair []. It has also been shown to bind DNA and physically interacts with RAD51 []. Biallelic mutations in PALB2 cause Fanconi anemia (FA) subtype FA-N, whereas monoallelic mutations predispose to breast, and pancreatic familial cancers[].
Protein Domain
Type: Family
Description: RFWD3 is a RING-type E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage [, , ].During ICL repair, single-stranded DNA (ssDNA) is generated. The trimeric ssDNA binding protein complex RPA coats the ssDNA. Subsequently, RAD51 is loaded onto RPA-bound ssDNA and catalyzes the critical activity in homologous recombination (HR). RFWD3 polyubiquitinates both RPA and RAD5, which increases their local turnover in DNA damage-induced foci to facilitate HR []. RFWD3-mediated ubiquitination of RPA has been shown to be essential for HR [].
Publication
First Author: Orelli BJ
Year: 2001
Journal: Breast Cancer Res
Title: BRCA2 and homologous recombination.
Volume: 3
Issue: 5
Pages: 294-8
Protein
Organism: Mus musculus/domesticus
Length: 319  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 303  
Fragment?: false
Publication
First Author: Yuan J
Year: 2011
Journal: J Biol Chem
Title: The role of the human SWI5-MEI5 complex in homologous recombination repair.
Volume: 286
Issue: 11
Pages: 9888-93
Publication
First Author: Walker LC
Year: 2010
Journal: Hum Mutat
Title: Detection of splicing aberrations caused by BRCA1 and BRCA2 sequence variants encoding missense substitutions: implications for prediction of pathogenicity.
Volume: 31
Issue: 6
Pages: E1484-505
Publication
First Author: Cohen-Tannoudji M
Year: 2000
Journal: Genomics
Title: A 2-Mb YAC/BAC-based physical map of the ovum mutant (Om) locus region on mouse chromosome 11.
Volume: 68
Issue: 3
Pages: 273-82
Protein
Organism: Mus musculus/domesticus
Length: 3329  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 3329  
Fragment?: false
Publication
First Author: Sun W
Year: 2008
Journal: Mol Cell
Title: The FANCM ortholog Fml1 promotes recombination at stalled replication forks and limits crossing over during DNA double-strand break repair.
Volume: 32
Issue: 1
Pages: 118-28
Publication
First Author: Nandi S
Year: 2012
Journal: Nucleic Acids Res
Title: The ATPase activity of Fml1 is essential for its roles in homologous recombination and DNA repair.
Volume: 40
Issue: 19
Pages: 9584-95
Publication
First Author: Chen YH
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Interplay between the Smc5/6 complex and the Mph1 helicase in recombinational repair.
Volume: 106
Issue: 50
Pages: 21252-7