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Search results 201 to 243 out of 243 for Eme1

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Type Details Score
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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UniProt Feature
UniProt Feature
Begin: 1
Description: Crossover junction endonuclease EME1
Type: chain
End: 570
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Protein
Q8BJW7
Organism: Mus musculus/domesticus
Length: 570  
Fragment?: false
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Publication
14609959 | -
First Author: Abraham J
Year: 2003
Journal: EMBO J
Title: Eme1 is involved in DNA damage processing and maintenance of genomic stability in mammalian cells.
Volume: 22
Issue: 22
Pages: 6137-47
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Interaction Experiment
Mistry H (2008)
Description: Interplay between Np95 and Eme1 in the DNA damage response.
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Publication
27010503 | J:235782
First Author: Braun J
Year: 2016
Journal: PLoS One
Title: The GIY-YIG Type Endonuclease Ankyrin Repeat and LEM Domain-Containing Protein 1 (ANKLE1) Is Dispensable for Mouse Hematopoiesis.
Volume: 11
Issue: 3
Pages: e0152278
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Protein Domain
IPR006166 | ERCC4_domain
Type: Domain
Description: This entry represents a structural domain found in several DNA repair nucleases, such as Rad1, XPF and crossover junction endonucleases EME1 and Mus81 [, ]. The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essential for maintaining genome stability. The nuclease domain architecture exhibits remarkable similarity to those of restriction endonucleases.
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Publication
12679022 | -
First Author: Nishino T
Year: 2003
Journal: Structure
Title: X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease: similarity between its endonuclease domain and restriction enzymes.
Volume: 11
Issue: 4
Pages: 445-57
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Publication
14527419 | -
First Author: Gaillard PH
Year: 2003
Journal: Mol Cell
Title: The endogenous Mus81-Eme1 complex resolves Holliday junctions by a nick and counternick mechanism.
Volume: 12
Issue: 3
Pages: 747-59
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Protein Domain
IPR042530 | EME1/EME2_C
Type: Homologous_superfamily
Description: This superfamily includes the C-terminal domain found in Eme1 from fission yeasts, and EME1/EME2 from animals. They interact with Mus81 to from a complex, which acts as a structure-specific endonuclease that targets branched DNA structures with a 5'-end at the branch nick [, ]. The typical substrates of this complex include 3'-flap structures, replication forks and nicked Holliday junctions [, ].Similar to MUS81-EME1, human MUS81-EME2 cleaves 3'-flaps, replication forks and nicked Holliday junctions, and exhibits limited endonuclease activity with intact Holliday junctions. However, MUS81-EME2 can also cleave a variety of DNA structures including D-loop recombination intermediates and nicked duplex [, ].Both Mus81 and Eme1 consist of a central nuclease domain, two repeats of the helix-hairpin-helix (HhH) motif at their C-terminal region, and a linker helix [].
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Protein Domain
IPR043087 | Eme1_nucdom_sub2
Type: Homologous_superfamily
Description: The Mus81-Eme1 complex is a structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the meiotic recombination intermediates in eukaryotes. Mus81 and Eme1 consist of a central nuclease domain, two repeats of the helix-hairpin-helix (HhH) motif at their C-terminal region, and a linker helix.The nuclease domain is found in several DNA repair nucleases, including Rad1, XPF and crossover junction endonucleases EME1 (an essential component of a Holliday junction resolvase) and Mus81 [, ]. The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essential for maintaining genome stability. The nuclease domain architecture exhibits remarkable similarity to those of restriction endonucleases.This superfamily consists of the second subdomain of the nuclease domain found in EME1.
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Protein Domain
IPR043086 | EME1_nucdom_sub1
Type: Homologous_superfamily
Description: The Mus81-Eme1 complex is a structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the meiotic recombination intermediates in eukaryotes. Mus81 and Eme1 consist of a central nuclease domain, two repeats of the helix-hairpin-helix (HhH) motif at their C-terminal region, and a linker helix.The nuclease domain is found in several DNA repair nucleases, including Rad1, XPF and crossover junction endonucleases EME1 (an essential component of a Holliday junction resolvase) and Mus81 [, ]. The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essential for maintaining genome stability. The nuclease domain architecture exhibits remarkable similarity to those of restriction endonucleases.This superfamily consists of the first part of the nuclease domain found in EME1.
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Protein
Q56A04
Organism: Mus musculus/domesticus
Length: 373  
Fragment?: false
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Protein
D3Z6X0
Organism: Mus musculus/domesticus
Length: 352  
Fragment?: false
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Publication
14642571 | -
First Author: Fu Y
Year: 2003
Journal: DNA Repair (Amst)
Title: Functional domains required for the Saccharomyces cerevisiae Mus81-Mms4 endonuclease complex formation and nuclear localization.
Volume: 2
Issue: 12
Pages: 1435-47
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Publication
17363897 | -
First Author: Gaskell LJ
Year: 2007
Journal: EMBO J
Title: Mus81 cleavage of Holliday junctions: a failsafe for processing meiotic recombination intermediates?
Volume: 26
Issue: 7
Pages: 1891-901
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Publication
26273056 | -
First Author: Mayle R
Year: 2015
Journal: Science
Title: DNA REPAIR. Mus81 and converging forks limit the mutagenicity of replication fork breakage.
Volume: 349
Issue: 6249
Pages: 742-7
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Publication
22551069 | -
First Author: Shin YK
Year: 2012
Journal: FEBS J
Title: Human MUS81 complexes stimulate flap endonuclease 1.
Volume: 279
Issue: 13
Pages: 2412-30
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Publication
24371268 | -
First Author: Pepe A
Year: 2014
Journal: Nucleic Acids Res
Title: Substrate specificity of the MUS81-EME2 structure selective endonuclease.
Volume: 42
Issue: 6
Pages: 3833-45
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Publication
24692662 | -
First Author: Amangyeld T
Year: 2014
Journal: Nucleic Acids Res
Title: Human MUS81-EME2 can cleave a variety of DNA structures including intact Holliday junction and nicked duplex.
Volume: 42
Issue: 9
Pages: 5846-62
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Protein
D6RIK4
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: false
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Protein Domain
IPR033310 | Mms4/EME1/EME2
Type: Family
Description: This entry includes Mms4 from budding yeast, Eme1 from fission yeasts, and EME1/EME2 from animals. They interact with Mus81 to from a complex, which acts as a structure-specific endonuclease that targets branched DNA structures with a 5'-end at the branch nick [, ]. The typical substrates of this complex include 3'-flap structures, replication forks and nicked Holliday junctions [, ].Similar to MUS81-EME1, human MUS81-EME2 cleaves 3'-flaps, replication forks and nicked Holliday junctions, and exhibits limited endonuclease activity with intact Holliday junctions. However, MUS81-EME2 can also cleave a variety of DNA structures including D-loop recombination intermediates and nicked duplex [, ].
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Protein
A0A494BB15
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: true
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Publication
19026666 | J:144039
First Author: Tamblyn L
Year: 2009
Journal: Mutat Res
Title: A role for Mus81 in the repair of chromium-induced DNA damage.
Volume: 660
Issue: 1-2
Pages: 57-65
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Protein
Q91ZJ0
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
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Protein
F8WIN9
Organism: Mus musculus/domesticus
Length: 502  
Fragment?: false
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Protein
A0A1Y7VKY9
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: true
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Protein
Q9QZD4
Organism: Mus musculus/domesticus
Length: 917  
Fragment?: false
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Protein
Q8CE63
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
Q3TRW6
Organism: Mus musculus/domesticus
Length: 401  
Fragment?: true
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Protein
F6VIY4
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: true
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Protein
Q8BGE5
Organism: Mus musculus/domesticus
Length: 2021  
Fragment?: false
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Protein
B2RX10
Organism: Mus musculus/domesticus
Length: 2021  
Fragment?: false
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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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
21183079 | J:292518
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89
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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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