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 []. |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1238
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
734
 |
Fragment?: |
true |
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•
•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1198
 |
Fragment?: |
false |
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•
•
•
•
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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 |
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•
•
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•
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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 |
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•
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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 |
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HT Experiment |
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Experiment Type: |
RNA-Seq |
Study Type: |
WT vs. Mutant |
Source: |
GEO |
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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 |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
201
 |
Fragment?: |
false |
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•
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•
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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 |
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•
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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 |
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•
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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 |
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•
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•
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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 |
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•
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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 |
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•
•
•
•
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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 |
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•
•
•
•
•
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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 |
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•
•
•
•
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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 |
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•
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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 |
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•
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•
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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 |
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•
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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 |
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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 []. |
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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[]. |
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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 []. |
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Publication |
First Author: |
Orelli BJ |
Year: |
2001 |
Journal: |
Breast Cancer Res |
Title: |
BRCA2 and homologous recombination. |
Volume: |
3 |
Issue: |
5 |
Pages: |
294-8 |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
319
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
303
 |
Fragment?: |
false |
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•
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•
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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 |
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•
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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 |
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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 |
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•
•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
3329
 |
Fragment?: |
false |
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•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
3329
 |
Fragment?: |
false |
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•
•
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•
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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 |
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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 |
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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 |
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