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Search results 101 to 200 out of 206 for Rev1

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Type Details Score
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: DNA repair protein REV1
Type: chain
End: 1249
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Protein
A0A0A6YX77
Organism: Mus musculus/domesticus
Length: 82  
Fragment?: true
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Protein
A0A0A6YX32
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: true
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Protein
A0A0A6YW35
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Protein
A0A0A6YWQ5
Organism: Mus musculus/domesticus
Length: 22  
Fragment?: true
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Protein
A0A0A6YWI0
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: true
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Publication
26187992 | J:233042
First Author: Yang Y
Year: 2015
Journal: Nucleic Acids Res
Title: FANCD2 and REV1 cooperate in the protection of nascent DNA strands in response to replication stress.
Volume: 43
Issue: 17
Pages: 8325-39
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Pathway
R-MMU-110312 | Translesion synthesis by REV1
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Interaction Experiment
Guo C (2006)
Description: REV1 protein interacts with PCNA: significance of the REV1 BRCT domain in vitro and in vivo.
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Interaction Experiment
Wang Z (2016)
Description: REV1 promotes PCNA monoubiquitination through interacting with ubiquitinated RAD18.
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Publication
22859296 | -
First Author: Kikuchi S
Year: 2012
Journal: J Biol Chem
Title: Structural basis of recruitment of DNA polymerase ζ by interaction between REV1 and REV7 proteins.
Volume: 287
Issue: 40
Pages: 33847-52
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Publication
15588843 | -
 
First Author: Lawrence CW
Year: 2004
Journal: Adv Protein Chem
Title: Cellular functions of DNA polymerase zeta and Rev1 protein.
Volume: 69
Pages: 167-203
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Publication
12509231 | -
First Author: Lawrence CW
Year: 2002
Journal: DNA Repair (Amst)
Title: Cellular roles of DNA polymerase zeta and Rev1 protein.
Volume: 1
Issue: 6
Pages: 425-35
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Publication
26795561 | -
First Author: Wang Z
Year: 2016
Journal: J Cell Sci
Title: REV1 promotes PCNA monoubiquitylation through interacting with ubiquitylated RAD18.
Volume: 129
Issue: 6
Pages: 1223-33
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Interaction Experiment
Guo C (2006)
Description: Ubiquitin-binding motifs in REV1 protein are required for its role in the tolerance of DNA damage.
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Interaction Experiment
Guo C (2003)
Description: Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis.
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Interaction Experiment
Gabel SA (2013)
Description: XRCC1 interaction with the REV1 C-terminal domain suggests a role in post replication repair.
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Interaction Experiment
Shim HS (2015)
Description: Starvation promotes REV1 SUMOylation and p53-dependent sensitization of melanoma and breast cancer cells.
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Interaction Experiment
Niu X (2019)
Description: Rev1 plays central roles in mammalian DNA-damage tolerance in response to UV irradiation.
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Publication
18603483 | -
First Author: D'Souza S
Year: 2008
Journal: DNA Repair (Amst)
Title: Novel conserved motifs in Rev1 C-terminus are required for mutagenic DNA damage tolerance.
Volume: 7
Issue: 9
Pages: 1455-70
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Publication
22691049 | -
First Author: Pozhidaeva A
Year: 2012
Journal: Biochemistry
Title: NMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase η.
Volume: 51
Issue: 27
Pages: 5506-20
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Publication
11356151 | -
First Author: Lawrence CW
Year: 2001
Journal: Biochem Soc Trans
Title: Eukaryotic mutagenesis and translesion replication dependent on DNA polymerase zeta and Rev1 protein.
Volume: 29
Issue: Pt 2
Pages: 187-91
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Publication
24409475 | -
First Author: Gabel SA
Year: 2013
Journal: DNA Repair (Amst)
Title: XRCC1 interaction with the REV1 C-terminal domain suggests a role in post replication repair.
Volume: 12
Issue: 12
Pages: 1105-13
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Publication
25614517 | -
First Author: Shim HS
Year: 2015
Journal: Cancer Res
Title: Starvation promotes REV1 SUMOylation and p53-dependent sensitization of melanoma and breast cancer cells.
Volume: 75
Issue: 6
Pages: 1056-67
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Publication
30963698 | -
First Author: Niu X
Year: 2019
Journal: FEBS J
Title: Rev1 plays central roles in mammalian DNA-damage tolerance in response to UV irradiation.
Volume: 286
Issue: 14
Pages: 2711-2725
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Publication
18242152 | -
First Author: Kosarek JN
Year: 2008
Journal: DNA Repair (Amst)
Title: Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts.
Volume: 7
Issue: 3
Pages: 439-51
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Protein Coding Gene
MGI:1337131 | Rev3l
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1919140 | Mad2l2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q9D752
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
Q61493
Organism: Mus musculus/domesticus
Length: 3122  
Fragment?: false
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Protein Domain
IPR031991 | Rev1_C
Type: Domain
Description: This entry represents the C-terminal domain of DNA repair protein Rev1, an enzyme which allows DNA synthesis to proceed even in the presence of DNA damage. Rev1 belongs to the Y-family of TLS polymerases. Rev1 possess a limited catalytic activity but it has a second and more important function which involved the recruitment and coordination of other Y-family TLS polymerases and the regulatory subunit Rev7 of the B-family polymerase pol. This interaction is mediated by its C-terminal domain which therefore serves as a scaffold that allows access of the Y-family polymerases to their cognate DNA lesions and the subsequent exchange to pol, which then extends the distorted DNA primer terminus opposite the lesion [, ]. This domain adopts a four-helix bundle that interacts with Rev7, Polkappa and Poleta. However, the Rev7-binding interface is distinct from the binding site of DNA polymerase eta or kappa [, ].
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Protein Domain
IPR038401 | Rev1_C_sf
Type: Homologous_superfamily
Description: This entry represents the C-terminal domain of DNA repair protein Rev1, an enzyme which allows DNA synthesis to proceed even in the presence of DNA damage. Rev1 belongs to the Y-family of TLS polymerases. Rev1 possess a limited catalytic activity but it has a second and more important function which involved the recruitment and coordination of other Y-family TLS polymerases and the regulatory subunit Rev7 of the B-family polymerase pol. This interaction is mediated by its C-terminal domain which therefore serves as a scaffold that allows access of the Y-family polymerases to their cognate DNA lesions and the subsequent exchange to pol, which then extends the distorted DNA primer terminus opposite the lesion [, ]. This domain adopts a four-helix bundle that interacts with Rev7, Polkappa and Poleta. However, the Rev7-binding interface is distinct from the binding site of DNA polymerase eta or kappa [, ].
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Publication
29669924 | J:262069
First Author: Thientosapol ES
Year: 2018
Journal: Proc Natl Acad Sci U S A
Title: SAMHD1 enhances immunoglobulin hypermutation by promoting transversion mutation.
Volume: 115
Issue: 19
Pages: 4921-4926
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Publication
10518552 | J:58083
First Author: Gerlach VL
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Human and mouse homologs of Escherichia coli DinB (DNA polymerase IV), members of the UmuC/DinB superfamily.
Volume: 96
Issue: 21
Pages: 11922-7
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Publication
9560379 | -
First Author: Smith BT
Year: 1998
Journal: Genetics
Title: Mutagenesis and more: umuDC and the Escherichia coli SOS response.
Volume: 148
Issue: 4
Pages: 1599-610
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Protein Domain
IPR001126 | UmuC
Type: Domain
Description: In Escherichia coli, UV and many chemicals appear to cause mutagenesis by a process of translesion synthesis that requires DNA polymerase III and the SOS-regulated proteins UmuD, UmuC and RecA. This machinery allows the replication to continuethrough DNA lesion, and therefore avoid lethal interruption of DNA replication after DNA damage []. UmuC is a well conserved protein in prokaryotes, with a homologue in yeast species.Proteins known to contain an UmuC domain are listed below: E. coli MucB protein. Plasmid-born analogue of the UmuC protein.Saccharomyces cerevisiae (Baker's yeast) Rev1 protein. Homologue of UmuC also required for normal induction of mutations by physical and chemical agents. Salmonella typhimurium ImpB protein. Plasmid-born analogue of the UmuC protein.Bacterial UmuC protein.E. coli DNA-damage-inducible protein P (DinP).S. typhimurium SamB homologue of UmuC plasmid associated.
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Publication
10620008 | J:59636
First Author: Ogi T
Year: 1999
Journal: Genes Cells
Title: Mutation enhancement by DINB1, a mammalian homologue of the Escherichia coli mutagenesis protein dinB.
Volume: 4
Issue: 11
Pages: 607-18
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Publication
11050393 | J:65200
First Author: Esposito G
Year: 2000
Journal: Curr Biol
Title: Disruption of the Rev3l-encoded catalytic subunit of polymerase zeta in mice results in early embryonic lethality.
Volume: 10
Issue: 19
Pages: 1221-4
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Publication
21068378 | J:167170
First Author: Xie K
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: Error-prone translesion synthesis mediates acquired chemoresistance.
Volume: 107
Issue: 48
Pages: 20792-7
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Publication
25799990 | J:222163
First Author: Boersma V
Year: 2015
Journal: Nature
Title: MAD2L2 controls DNA repair at telomeres and DNA breaks by inhibiting 5' end resection.
Volume: 521
Issue: 7553
Pages: 537-540
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Protein Coding Gene
MGI:2146571 | Rfc4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:97891 | Rfc1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1919401 | Rfc5
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1341868 | Rfc2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1916513 | Rfc3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q9D0F6
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
Q9WUK4
Organism: Mus musculus/domesticus
Length: 349  
Fragment?: false
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Protein
Q8R323
Organism: Mus musculus/domesticus
Length: 356  
Fragment?: false
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Protein
P35601
Organism: Mus musculus/domesticus
Length: 1131  
Fragment?: false
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Protein
Q99J62
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: false
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Protein
A0A1Y7VJV3
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true
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Protein
E0CZD6
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
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Protein
Q3UUL1
Organism: Mus musculus/domesticus
Length: 239  
Fragment?: true
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Protein
A0A3B2WAL6
Organism: Mus musculus/domesticus
Length: 102  
Fragment?: false
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Protein
Q5Q9H3
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
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Protein Domain
IPR036775 | DNA_pol_Y-fam_lit_finger_sf
Type: Homologous_superfamily
Description: This entry represents the little finger domain superfamily found in Y-family (lesion bypass) DNA polymerases. Y-family polymerases were originally known as UmuC/DinB/Rev1/Rad30 after each branch of the family. These enzymes are characterised by their low-fidelity synthesis on undamaged DNA templates and by their ability to traverse replication-blocking lesions. By contrast, high-fidelity polymerases (such as DNA polymerase III) are sensitive to distortions in the DNA template. As a result, Y-family polymerases can extend primer strands across DNA strand lesions that would otherwise stall replicative polymerases. To minimize mutations through their low fidelity synthesis, these enzymes are regulated, and are thought to interact with processivity factors, β-clamp or proliferating cell nuclear antigen (PCNA), which are also essential for the function of replicative DNA polymerases []. Organisms can contain more than one Y-family polymerase, each with a unique DNA damage bypass and fidelity profile. For example, humans posses four Y-family polymerases: DNA polymerases kappa, iota, eta and Rev1. Y-family polymerases show no homology to DNA polymerases from the A-, B-, C-, D- or X-families []. The Y-family of DNA polymerases includes the following enzymes:Prokaryotic DNA polymerase IV (DinB) [].Archaeal DinB homologue DNA polymerase IV [].Eukaryotic DinB homologue DNA polymerase kappa [].Prokarytoic DNA repair proteins UmuC and UmuD [].Eukaryotic Rad30 homologues DNA polymerase eta and iota [, ].Eukaryotic DNA repair protein Rev1 [].Human DNA polymerase kappa is a right-handed shaped molecule with palm, fingers, thumb, little finger and wrist subdomains []. The little finger domain has a beta-α-β(2)-α-β fold with antiparallel β-sheet and a reversed ferredoxin-like topology.
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Protein Domain
IPR017961 | DNA_pol_Y-fam_little_finger
Type: Domain
Description: This entry represents the little finger domain found in Y-family (lesion bypass) DNA polymerases. Y-family polymerases were originally known as UmuC/DinB/Rev1/Rad30 after each branch of the family. These enzymes are characterised by their low-fidelity synthesis on undamaged DNA templates and by their ability to traverse replication-blocking lesions. By contrast, high-fidelity polymerases (such as DNA polymerase III) are sensitive to distortions in the DNA template. As a result, Y-family polymerases can extend primer strands across DNA strand lesions that would otherwise stall replicative polymerases. To minimize mutations through their low fidelity synthesis, these enzymes are regulated, and are thought to interact with processivity factors, β-clamp or proliferating cell nuclear antigen (PCNA), which are also essential for the function of replicative DNA polymerases []. Organisms can contain more than one Y-family polymerase, each with a unique DNA damage bypass and fidelity profile. For example, humans posses four Y-family polymerases: DNA polymerases kappa, iota, eta and Rev1. Y-family polymerases show no homology to DNA polymerases from the A-, B-, C-, D- or X-families []. The Y-family of DNA polymerases includes the following enzymes:Prokaryotic DNA polymerase IV (DinB) [].Archaeal DinB homologue DNA polymerase IV [].Eukaryotic DinB homologue DNA polymerase kappa [].Prokarytoic DNA repair proteins UmuC and UmuD [].Eukaryotic Rad30 homologues DNA polymerase eta and iota [, ].Eukaryotic DNA repair protein Rev1 [].Human DNA polymerase kappa is a right-handed shaped molecule with palm, fingers, thumb, little finger and wrist subdomains [].
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Publication
21931560 | J:177283
First Author: Hendel A
Year: 2011
Journal: PLoS Genet
Title: PCNA ubiquitination is important, but not essential for translesion DNA synthesis in mammalian cells.
Volume: 7
Issue: 9
Pages: e1002262
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Protein Coding Gene
MGI:1915525 | Rpa1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:97503 | Pcna
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1339939 | Rpa2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1915490 | Rpa3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P17918
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: false
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Protein
Q9CQ71
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
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Protein
Q62193
Organism: Mus musculus/domesticus
Length: 270  
Fragment?: false
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Protein
Q8VEE4
Organism: Mus musculus/domesticus
Length: 623  
Fragment?: false
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Publication
11545743 | -
First Author: Trincao J
Year: 2001
Journal: Mol Cell
Title: Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis.
Volume: 8
Issue: 2
Pages: 417-26
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Publication
11595188 | -
First Author: Ling H
Year: 2001
Journal: Cell
Title: Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication.
Volume: 107
Issue: 1
Pages: 91-102
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Publication
15296733 | -
First Author: Uljon SN
Year: 2004
Journal: Structure
Title: Crystal structure of the catalytic core of human DNA polymerase kappa.
Volume: 12
Issue: 8
Pages: 1395-404
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Publication
14592985 | -
First Author: Bunting KA
Year: 2003
Journal: EMBO J
Title: Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp.
Volume: 22
Issue: 21
Pages: 5883-92
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Publication
16819516 | -
First Author: Nair DT
Year: 2006
Journal: Nat Struct Mol Biol
Title: Hoogsteen base pair formation promotes synthesis opposite the 1,N6-ethenodeoxyadenosine lesion by human DNA polymerase iota.
Volume: 13
Issue: 7
Pages: 619-25
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Publication
17207624 | -
First Author: Jarosz DF
Year: 2007
Journal: Trends Microbiol
Title: Y-family DNA polymerases in Escherichia coli.
Volume: 15
Issue: 2
Pages: 70-7
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Protein
Q3TQ92
Organism: Mus musculus/domesticus
Length: 267  
Fragment?: true
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Protein
Q5Q9H4
Organism: Mus musculus/domesticus
Length: 275  
Fragment?: false
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Protein
Q6R3M4
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
Q9JJN0
Organism: Mus musculus/domesticus
Length: 694  
Fragment?: false
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Protein
Q3ULX6
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
A0A0R4J1Z5
Organism: Mus musculus/domesticus
Length: 674  
Fragment?: false
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Protein
G8DM24
Organism: Mus musculus/domesticus
Length: 737  
Fragment?: false
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Protein
Q5Q9H1
Organism: Mus musculus/domesticus
Length: 547  
Fragment?: false
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Protein
I6L9K1
Organism: Mus musculus/domesticus
Length: 556  
Fragment?: false
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Protein
A0A1Y7VIV8
Organism: Mus musculus/domesticus
Length: 547  
Fragment?: false
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Protein
Q5Q9H2
Organism: Mus musculus/domesticus
Length: 495  
Fragment?: false
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Protein
Q5Q9H8
Organism: Mus musculus/domesticus
Length: 533  
Fragment?: false
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Protein
Q3U3X3
Organism: Mus musculus/domesticus
Length: 549  
Fragment?: false
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Protein
E9Q3H9
Organism: Mus musculus/domesticus
Length: 651  
Fragment?: false
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Protein
G8DM25
Organism: Mus musculus/domesticus
Length: 737  
Fragment?: false
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Protein
E9QJU6
Organism: Mus musculus/domesticus
Length: 737  
Fragment?: false
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Protein
G8DM28
Organism: Mus musculus/domesticus
Length: 737  
Fragment?: false
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Protein
Q5Q9H0
Organism: Mus musculus/domesticus
Length: 467  
Fragment?: false
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Protein
Q5Q9H5
Organism: Mus musculus/domesticus
Length: 453  
Fragment?: false
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Protein
Q9QUG2
Organism: Mus musculus/domesticus
Length: 852  
Fragment?: false
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Protein
Q5Q9H6
Organism: Mus musculus/domesticus
Length: 772  
Fragment?: false
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Protein
Q5Q9H7
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
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Protein
Q5Q9G9
Organism: Mus musculus/domesticus
Length: 434  
Fragment?: false
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Protein Coding Gene
MGI:1925544 | Rps27a
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98887 | Uba52
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98888 | Ubb
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98889 | Ubc
Type: protein_coding_gene
Organism: mouse, laboratory
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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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom