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Search results 101 to 169 out of 169 for Msh3

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Type Details Score
Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Protein
Q8CGC9
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
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UniProt Feature
UniProt Feature
Begin: 1
Description: DNA mismatch repair protein Msh3
Type: chain
End: 1091
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Publication
37177784 | J:359526
First Author: O'Reilly D
Year: 2023
Journal: Mol Ther
Title: Di-valent siRNA-mediated silencing of MSH3 blocks somatic repeat expansion in mouse models of Huntington's disease.
Volume: 31
Issue: 6
Pages: 1661-1674
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Protein
A0A087WQZ2
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: true
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Protein
A0A087WSS2
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: false
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Protein
P13705
Organism: Mus musculus/domesticus
Length: 1091  
Fragment?: false
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Protein
A0A087WRJ5
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
A0A087WP43
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: false
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Protein
A0A087WP45
Organism: Mus musculus/domesticus
Length: 167  
Fragment?: false
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Protein
A0A087WSR8
Organism: Mus musculus/domesticus
Length: 56  
Fragment?: false
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Publication
8510668 | -
First Author: New L
Year: 1993
Journal: Mol Gen Genet
Title: The yeast gene MSH3 defines a new class of eukaryotic MutS homologues.
Volume: 239
Issue: 1-2
Pages: 97-108
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HT Experiment
GSE237564 | Transcriptional profiling of cortex from a mouse model of Huntington's disease (Q140) crossed with Msh3 heterozygous and homozygous mice [Msh3_cortex_6m]
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE237571 | Transcriptional profiling of striatum from a mouse model of Huntington's disease (Q140) crossed with Msh3 heterozygous and homozygous mice [Msh3_striatum_6m]
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE229827 | Transcriptional profiling of striatum from a mouse model of Huntington's disease (Q140) crossed with Msh3 heterozygous and homozygous mice [Msh3_striatum]
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE241278 | Transcriptional profiling of striatum from a mouse model of Huntington's disease (Q140) crossed with Msh3 heterozygous and homozygous mice [Msh3 snRNA-seq]
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE229826 | Transcriptional profiling of cerebral cortex from a mouse model of Huntington's disease (Q140) crossed with Msh3 heterozygous and homozygous mice [Msh3_cortex]
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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DO Term
DOID:0080412 | familial adenomatous polyposis 4
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Publication
10644444 | J:60262
First Author: Geeta Vani R
Year: 1999
Journal: Genomics
Title: Cloning of rat MLH1 and expression analysis of MSH2, MSH3, MSH6, and MLH1 during spermatogenesis.
Volume: 62
Issue: 3
Pages: 460-7
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Publication
37315918 | J:360449
 
First Author: Bai D
Year: 2023
Journal: Prog Neurobiol
Title: Loss of TDP-43 promotes somatic CAG repeat expansion in Huntington's disease knock-in mice.
Volume: 227
Pages: 102484
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Publication
39938516 | J:361636
     
First Author: Wang N
Year: 2025
Journal: Cell
Title: Distinct mismatch-repair complex genes set neuronal CAG-repeat expansion rate to drive selective pathogenesis in HD mice.
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Publication
12091911 | J:78200
First Author: Lipkin SM
Year: 2002
Journal: Nat Genet
Title: Meiotic arrest and aneuploidy in MLH3-deficient mice.
Volume: 31
Issue: 4
Pages: 385-90
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Publication
24204323 | J:205134
First Author: Pinto RM
Year: 2013
Journal: PLoS Genet
Title: Mismatch repair genes Mlh1 and Mlh3 modify CAG instability in Huntington's disease mice: genome-wide and candidate approaches.
Volume: 9
Issue: 10
Pages: e1003930
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Protein Domain
IPR000432 | DNA_mismatch_repair_MutS_C
Type: Domain
Description: Mismatch repair contributes to the overall fidelity of DNA replication and is essential for combating the adverse effects of damage to the genome. It involves the correction of mismatched base pairs that have been missed by the proofreading element of the DNA polymerase complex. The post-replicative Mismatch Repair System (MMRS) of Escherichia coli involves MutS (Mutator S), MutL and MutH proteins, and acts to correct point mutations or small insertion/deletion loops produced during DNA replication []. MutS and MutL are involved in preventing recombination between partially homologous DNA sequences. The assembly of MMRS is initiated by MutS, which recognises and binds to mispaired nucleotides and allows further action of MutL and MutH to eliminate a portion of newly synthesized DNA strand containing the mispaired base []. MutS can also collaborate with methyltransferases in the repair of O(6)-methylguanine damage, which would otherwise pair with thymine during replication to create an O(6)mG:T mismatch []. MutS exists as a dimer, where the two monomers have different conformations and form a heterodimer at the structural level []. Only one monomer recognises the mismatch specifically and has ADP bound. Non-specific major groove DNA-binding domains from both monomers embrace the DNA in a clamp-like structure. Mismatch binding induces ATP uptake and a conformational change in the MutS protein, resulting in a clamp that translocates on DNA. MutS is a modular protein with a complex structure [], and is composed of:N-terminal mismatch-recognition domain, which is similar in structure to tRNA endonuclease.Connector domain, which is similar in structure to Holliday junction resolvase ruvC.Core domain, which is composed of two separate subdomains that join together to form a helical bundle; from within the core domain, two helices act as levers that extend towards (but do not touch) the DNA.Clamp domain, which is inserted between the two subdomains of the core domain at the top of the lever helices; the clamp domain has a β-sheet structure.ATPase domain (connected to the core domain), which has a classical Walker A motif.HTH (helix-turn-helix) domain, which is involved in dimer contacts.The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair. Homologues of MutS have been found in many species including eukaryotes (MSH 1, 2, 3, 4, 5, and 6 proteins), archaea and bacteria, and together these proteins have been grouped into the MutS family. Although many of these proteins have similar activities to the E. coli MutS, there is significant diversity of function among the MutS family members. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein [].This diversity is even seen within species, where many species encode multiple MutS homologues with distinct functions []. Inter-species homologues may have arisen through frequent ancient horizontal gene transfer of MutS (and MutL) from bacteria to archaea and eukaryotes via endosymbiotic ancestors of mitochondria and chloroplasts []. This entry represents the C-terminal domain found in proteins in the MutS family of DNA mismatch repair proteins. The C-terminal region of MutS is comprised of the ATPase domain and the HTH (helix-turn-helix)domain, the latter being involved in dimer contacts. Yeast MSH3 [], bacterial proteins involved in DNA mismatch repair, and the predicted protein product of the Rep-3 gene of mouse share extensive sequence similarity. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein.
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Protein Domain
IPR007695 | DNA_mismatch_repair_MutS-lik_N
Type: Domain
Description: Mismatch repair contributes to the overall fidelity of DNA replication and is essential for combating the adverse effects of damage to the genome. It involves the correction of mismatched base pairs that have been missed by the proofreading element of the DNA polymerase complex. The post-replicative Mismatch Repair System (MMRS) of Escherichia coli involves MutS (Mutator S), MutL and MutH proteins, and acts to correct point mutations or small insertion/deletion loops produced during DNA replication []. MutS and MutL are involved in preventing recombination between partially homologous DNA sequences. The assembly of MMRS is initiated by MutS, which recognises and binds to mispaired nucleotides and allows further action of MutL and MutH to eliminate a portion of newly synthesized DNA strand containing the mispaired base []. MutS can also collaborate with methyltransferases in the repair of O(6)-methylguanine damage, which would otherwise pair with thymine during replication to create an O(6)mG:T mismatch []. MutS exists as a dimer, where the two monomers have different conformations and form a heterodimer at the structural level []. Only one monomer recognises the mismatch specifically and has ADP bound. Non-specific major groove DNA-binding domains from both monomers embrace the DNA in a clamp-like structure. Mismatch binding induces ATP uptake and a conformational change in the MutS protein, resulting in a clamp that translocates on DNA. MutS is a modular protein with a complex structure [], and is composed of:N-terminal mismatch-recognition domain, which is similar in structure to tRNA endonuclease.Connector domain, which is similar in structure to Holliday junction resolvase ruvC.Core domain, which is composed of two separate subdomains that join together to form a helical bundle; from within the core domain, two helices act as levers that extend towards (but do not touch) the DNA.Clamp domain, which is inserted between the two subdomains of the core domain at the top of the lever helices; the clamp domain has a β-sheet structure.ATPase domain (connected to the core domain), which has a classical Walker A motif.HTH (helix-turn-helix) domain, which is involved in dimer contacts.The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair. Homologues of MutS have been found in many species including eukaryotes (MSH 1, 2, 3, 4, 5, and 6 proteins), archaea and bacteria, and together these proteins have been grouped into the MutS family. Although many of these proteins have similar activities to the E. coli MutS, there is significant diversity of function among the MutS family members. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein [].This diversity is even seen within species, where many species encode multiple MutS homologues with distinct functions []. Inter-species homologues may have arisen through frequent ancient horizontal gene transfer of MutS (and MutL) from bacteria to archaea and eukaryotes via endosymbiotic ancestors of mitochondria and chloroplasts []. This entry represents the N-terminal domain of proteins in the MutS family of DNA mismatch repair proteins, as well as closely related proteins. The N-terminal domain of MutS is responsible for mismatch recognition and forms a 6-stranded mixed β-sheet surrounded by three α-helices, which is similar to the structure of tRNA endonuclease. Yeast MSH3 [], bacterial proteins involved in DNA mismatch repair, and the predicted protein product of the Rep-3 gene of mouse share extensive sequence similarity. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein.
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Protein
Q7TNA0
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
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Protein
Q3TTD3
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: true
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Protein
Q9R1I5
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: true
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Protein
Q3V2Z1
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
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Protein
Q7TNA2
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: false
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Protein
Q8C9T6
Organism: Mus musculus/domesticus
Length: 190  
Fragment?: false
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Protein
Q7TNA5
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
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Protein
Q62156
Organism: Mus musculus/domesticus
Length: 394  
Fragment?: false
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Protein
G3UXD8
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: true
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Protein
P43247
Organism: Mus musculus/domesticus
Length: 935  
Fragment?: false
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Protein
E9QPY6
Organism: Mus musculus/domesticus
Length: 1094  
Fragment?: false
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Protein
Q3TZI5
Organism: Mus musculus/domesticus
Length: 935  
Fragment?: false
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Protein
B2RWY6
Organism: Mus musculus/domesticus
Length: 1095  
Fragment?: false
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Protein
Q80V79
Organism: Mus musculus/domesticus
Length: 935  
Fragment?: false
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Protein
A0A087WQ16
Organism: Mus musculus/domesticus
Length: 1095  
Fragment?: false
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Protein
P54276
Organism: Mus musculus/domesticus
Length: 1358  
Fragment?: false
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Protein
Q8C2N9
Organism: Mus musculus/domesticus
Length: 1358  
Fragment?: false
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Publication
9722651 | -
First Author: Eisen JA
Year: 1998
Journal: Nucleic Acids Res
Title: A phylogenomic study of the MutS family of proteins.
Volume: 26
Issue: 18
Pages: 4291-300
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Publication
8036718 | -
First Author: Jiricny J
Year: 1994
Journal: Trends Genet
Title: Colon cancer and DNA repair: have mismatches met their match?
Volume: 10
Issue: 5
Pages: 164-8
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Publication
11048711 | -
First Author: Lamers MH
Year: 2000
Journal: Nature
Title: The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch.
Volume: 407
Issue: 6805
Pages: 711-7
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Publication
17426027 | -
First Author: Mendillo ML
Year: 2007
Journal: J Biol Chem
Title: Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramers are essential for DNA mismatch repair in vivo.
Volume: 282
Issue: 22
Pages: 16345-54
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Publication
17919654 | -
First Author: Nag N
Year: 2007
Journal: J Mol Biol
Title: Altered dynamics of DNA bases adjacent to a mismatch: a cue for mismatch recognition by MutS.
Volume: 374
Issue: 1
Pages: 39-53
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Publication
17599803 | -
First Author: Miguel V
Year: 2007
Journal: Biochem Biophys Res Commun
Title: The C-terminal region of Escherichia coli MutS and protein oligomerization.
Volume: 360
Issue: 2
Pages: 412-7
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Publication
17951114 | -
First Author: Rye PT
Year: 2008
Journal: DNA Repair (Amst)
Title: Mismatch repair proteins collaborate with methyltransferases in the repair of O(6)-methylguanine.
Volume: 7
Issue: 2
Pages: 170-6
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Publication
17965091 | -
First Author: Lin Z
Year: 2007
Journal: Nucleic Acids Res
Title: The origins and early evolution of DNA mismatch repair genes--multiple horizontal gene transfers and co-evolution.
Volume: 35
Issue: 22
Pages: 7591-603
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Protein
Q99MT2
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
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Protein
Q9QUM7
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
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Protein
Q7TNA7
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
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Protein
B2RUF1
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
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Protein
A6H6D5
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
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Protein
A0A0R4IZY8
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
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Protein
A0A087WQN0
Organism: Mus musculus/domesticus
Length: 764  
Fragment?: false
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Protein
Q9CRH0
Organism: Mus musculus/domesticus
Length: 444  
Fragment?: true
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Protein
Q7TNA6
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
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Protein
A0A087WQG8
Organism: Mus musculus/domesticus
Length: 870  
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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Cambridge CB2 3EH, United Kingdom