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Search results 1 to 100 out of 443 for Eif4b

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Type Details Score
Gene
1975 | EIF4B
Type: gene
Organism: human
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Gene
505850 | EIF4B
Type: gene
Organism: cattle
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Gene
100858349 | EIF4B
Type: gene
Organism: chicken
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Gene
700688 | EIF4B
Type: gene
Organism: macaque, rhesus
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Gene
448618 | eif4b
Type: gene
Organism: frog, western clawed
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Gene
300253 | Eif4b
Type: gene
Organism: rat
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Gene
477600 | EIF4B
Type: gene
Organism: dog, domestic
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Gene
737509 | EIF4B
Type: gene
Organism: chimpanzee
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Protein Coding Gene
MGI:95304 | Eif4b
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
34566982 | J:311140
 
First Author: Chen B
Year: 2021
Journal: Front Immunol
Title: Deficiency of eIF4B Increases Mouse Mortality and Impairs Antiviral Immunity.
Volume: 12
Pages: 723885
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Publication
23105104 | J:193766
First Author: Dennis MD
Year: 2012
Journal: J Biol Chem
Title: Role of p70S6K1-mediated phosphorylation of eIF4B and PDCD4 proteins in the regulation of protein synthesis.
Volume: 287
Issue: 51
Pages: 42890-9
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Publication
19289497 | J:148986
First Author: Kroczynska B
Year: 2009
Journal: Mol Cell Biol
Title: Interferon-dependent engagement of eukaryotic initiation factor 4B via S6 kinase (S6K)- and ribosomal protein S6K-mediated signals.
Volume: 29
Issue: 10
Pages: 2865-75
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Protein Coding Gene
MGP_CAROLIEiJ_G0020335 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0022397 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0022359 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0022334 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0022363 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0022130 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_95304 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0022812 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0021656 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0022099 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0022230 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0022206 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0022299 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0022228 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0022824 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0021396 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0021706 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0020334 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0021228 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
- | J:238766
     
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
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Publication
10512203 | J:93290
First Author: Araki K
Year: 1999
Journal: Cell Mol Biol (Noisy-le-grand)
Title: Exchangeable gene trap using the Cre/mutated lox system.
Volume: 45
Issue: 5
Pages: 737-50
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Publication
15840001 | J:110088
First Author: Taniwaki T
Year: 2005
Journal: Dev Growth Differ
Title: Characterization of an exchangeable gene trap using pU-17 carrying a stop codon-beta geo cassette.
Volume: 47
Issue: 3
Pages: 163-72
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Publication
10725249 | J:60984
First Author: Ko MS
Year: 2000
Journal: Development
Title: Large-scale cDNA analysis reveals phased gene expression patterns during preimplantation mouse development.
Volume: 127
Issue: 8
Pages: 1737-49
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Publication
- | J:188991
     
First Author: The Jackson Laboratory
Year: 2012
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by The Jackson Laboratory
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Publication
12904583 | J:85162
First Author: Hansen J
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A large-scale, gene-driven mutagenesis approach for the functional analysis of the mouse genome.
Volume: 100
Issue: 17
Pages: 9918-22
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Publication
- | J:80155
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations for FANTOM2 data
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Publication
12520002 | J:91812
First Author: Stryke D
Year: 2003
Journal: Nucleic Acids Res
Title: BayGenomics: a resource of insertional mutations in mouse embryonic stem cells.
Volume: 31
Issue: 1
Pages: 278-81
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Publication
18799693 | J:142754
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
- | J:155856
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Rat to Mouse ISO GO annotation transfer
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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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
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:60000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
- | J:164563
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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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: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: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:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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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:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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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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Publication
25332164 | J:223882
First Author: Eom T
Year: 2014
Journal: J Cell Biol
Title: Neuronal BC RNAs cooperate with eIF4B to mediate activity-dependent translational control.
Volume: 207
Issue: 2
Pages: 237-52
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Publication
23749639 | J:199567
First Author: Yang J
Year: 2013
Journal: Cancer Res
Title: eIF4B phosphorylation by pim kinases plays a critical role in cellular transformation by Abl oncogenes.
Volume: 73
Issue: 15
Pages: 4898-908
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Allele
Eif4b<em2Smoc> | MGI:7289466
Name: eukaryotic translation initiation factor 4B; endonuclease-mediated mutation 2, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Allele
Eif4b<em1Smoc> | MGI:7289465
Name: eukaryotic translation initiation factor 4B; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Publication
23236192 | -
First Author: Walker SE
Year: 2013
Journal: RNA
Title: Yeast eIF4B binds to the head of the 40S ribosomal subunit and promotes mRNA recruitment through its N-terminal and internal repeat domains.
Volume: 19
Issue: 2
Pages: 191-207
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Publication
38011999 | J:344730
 
First Author: Screen M
Year: 2024
Journal: Life Sci Alliance
Title: RNA helicase EIF4A1-mediated translation is essential for the GC response.
Volume: 7
Issue: 2
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Publication
24777602 | J:223691
First Author: Cen B
Year: 2014
Journal: Mol Cell Biol
Title: The Pim-1 protein kinase is an important regulator of MET receptor tyrosine kinase levels and signaling.
Volume: 34
Issue: 13
Pages: 2517-32
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Publication
24945486 | J:216832
First Author: Steiner JL
Year: 2014
Journal: PLoS One
Title: Disruption of genes encoding eIF4E binding proteins-1 and -2 does not alter basal or sepsis-induced changes in skeletal muscle protein synthesis in male or female mice.
Volume: 9
Issue: 6
Pages: e99582
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Publication
22871496 | J:193228
First Author: Rico C
Year: 2012
Journal: Carcinogenesis
Title: Pharmacological targeting of mammalian target of rapamycin inhibits ovarian granulosa cell tumor growth.
Volume: 33
Issue: 11
Pages: 2283-92
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Publication
28584287 | J:345838
First Author: Kabir ZD
Year: 2017
Journal: Mol Psychiatry
Title: Rescue of impaired sociability and anxiety-like behavior in adult cacna1c-deficient mice by pharmacologically targeting eIF2α.
Volume: 22
Issue: 8
Pages: 1096-1109
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Publication
24829357 | J:214387
First Author: Wang S
Year: 2014
Journal: J Virol
Title: Influenza A virus-induced degradation of eukaryotic translation initiation factor 4B contributes to viral replication by suppressing IFITM3 protein expression.
Volume: 88
Issue: 15
Pages: 8375-85
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Publication
11087862 | -
First Author: Caruthers JM
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase.
Volume: 97
Issue: 24
Pages: 13080-5
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Publication
11839499 | -
First Author: Caruthers JM
Year: 2002
Journal: Curr Opin Struct Biol
Title: Helicase structure and mechanism.
Volume: 12
Issue: 1
Pages: 123-33
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Publication
11545728 | -
First Author: Tanner NK
Year: 2001
Journal: Mol Cell
Title: DExD/H box RNA helicases: from generic motors to specific dissociation functions.
Volume: 8
Issue: 2
Pages: 251-62
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Publication
8385320 | -
First Author: Koonin EV
Year: 1993
Journal: Nucleic Acids Res
Title: Escherichia coli dinG gene encodes a putative DNA helicase related to a group of eukaryotic helicases including Rad3 protein.
Volume: 21
Issue: 6
Pages: 1497
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Protein
Q5F0J9
Organism: Mus musculus/domesticus
Length: 34  
Fragment?: true
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Protein Domain
IPR014001 | Helicase_ATP-bd
Type: Domain
Description: Helicases have been classified in 5 superfamilies (SF1-SF5). All of the proteins bind ATP and, consequently, all of them carry the classical Walker A(phosphate-binding loop or P-loop) and Walker B(Mg2+-binding aspartic acid) motifs. For the two largest groups, commonlyreferred to as SF1 and SF2, a total of seven characteristic motifs has beenidentified []. These two superfamilies encompass a large number of DNA andRNA helicases from archaea, eubacteria, eukaryotes and viruses that seem to beactive as monomers or dimers. RNA and DNA helicases are considered to beenzymes that catalyze the separation of double-stranded nucleic acids in anenergy-dependent manner [].The various structures of SF1 and SF2 helicases present a common core with twoα-β RecA-like domains [, ]. Thestructural homology with the RecA recombination protein covers the fivecontiguous parallel beta strands and the tandem alpha helices. ATP binds tothe amino proximal α-β domain, where the Walker A (motif I) and WalkerB (motif II) are found. The N-terminal domain also contains motif III (S-A-T)which was proposed to participate in linking ATPase and helicase activities.The carboxy-terminal α-β domain is structurally very similar to theproximal one even though it is bereft of an ATP-binding site, suggesting thatit may have originally arisen through gene duplication of the first one.Some members of helicase superfamilies 1 and 2 are listed below:DEAD-box RNA helicases. The prototype of DEAD-boxproteins is the translation initiation factor eIF4A. The eIF4A protein isan RNA-dependent ATPase which functions together with eIF4B as an RNAhelicase [].DEAH-box RNA helicases. Mainly pre-mRNA-splicing factorATP-dependent RNA helicases [].Eukaryotic DNA repair helicase RAD3/ERCC-2, an ATP-dependent 5'-3' DNAhelicase involved in nucleotide excision repair of UV-damaged DNA.Eukaryotic TFIIH basal transcription factor complex helicase XPB subunit.An ATP-dependent 3'-5' DNA helicase which is a component of the core-TFIIHbasal transcription factor, involved in nucleotide excision repair (NER) ofDNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.It acts by opening DNA either around the RNA transcription start site orthe DNA.Eukaryotic ATP-dependent DNA helicase Q. A DNA helicase that may play arole in the repair of DNA that is damaged by ultraviolet light or othermutagens.Bacterial and eukaryotic antiviral SKI2-like helicase. SKI2 has a role inthe 3'-mRNA degradation pathway, repressing dsRNA virus propagation byspecifically blocking translation of viral mRNAs, perhaps recognizing theabsence of CAP or poly(A).Bacterial DNA-damage-inducible protein G (DinG). A probable helicaseinvolved in DNA repair and perhaps also replication [].Bacterial primosomal protein N' (PriA). PriA protein is one of sevenproteins that make up the restart primosome, an apparatus that promotesassembly of replisomes at recombination intermediates and stalledreplication forks.Bacterial ATP-dependent DNA helicase recG. It has a critical role inrecombination and DNA repair, helping process Holliday junctionintermediates to mature products by catalyzing branch migration. It has aDNA unwinding activity characteristic of helicases with a 3' to 5'polarity.A variety of DNA and RNA virus helicases and transcription factorsThis entry represents the DNA-binding domain of classical SF1 and SF2 helicases. It does not recognize bacterial DinG and eukaryotic Rad3 which differ from other SF1-SF2 helicases by the presence of a large insert after the Walker A (see ).
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Protein Domain
IPR014013 | Helic_SF1/SF2_ATP-bd_DinG/Rad3
Type: Domain
Description: Helicases have been classified in 5 superfamilies (SF1-SF5). All of the proteins bind ATP and, consequently, all of them carry the classical Walker A(phosphate-binding loop or P-loop) and Walker B(Mg2+-binding aspartic acid) motifs. For the two largest groups, commonlyreferred to as SF1 and SF2, a total of seven characteristic motifs has beenidentified []. These two superfamilies encompass a large number of DNA andRNA helicases from archaea, eubacteria, eukaryotes and viruses that seem to beactive as monomers or dimers. RNA and DNA helicases are considered to beenzymes that catalyze the separation of double-stranded nucleic acids in anenergy-dependent manner [].The various structures of SF1 and SF2 helicases present a common core with twoα-β RecA-like domains [, ]. Thestructural homology with the RecA recombination protein covers the fivecontiguous parallel beta strands and the tandem alpha helices. ATP binds tothe amino proximal α-β domain, where the Walker A (motif I) and WalkerB (motif II) are found. The N-terminal domain also contains motif III (S-A-T)which was proposed to participate in linking ATPase and helicase activities.The carboxy-terminal α-β domain is structurally very similar to theproximal one even though it is bereft of an ATP-binding site, suggesting thatit may have originally arisen through gene duplication of the first one.Some members of helicase superfamilies 1 and 2 are listed below:DEAD-box RNA helicases. The prototype ofDEAD-boxproteins is the translation initiation factor eIF4A. The eIF4A protein isan RNA-dependent ATPase which functions together with eIF4B as an RNAhelicase [].DEAH-box RNA helicases. Mainly pre-mRNA-splicing factorATP-dependent RNA helicases [].Eukaryotic DNA repair helicase RAD3/ERCC-2, an ATP-dependent 5'-3' DNAhelicase involved in nucleotide excision repair of UV-damaged DNA.Eukaryotic TFIIH basal transcription factor complex helicase XPB subunit.An ATP-dependent 3'-5' DNA helicase which is a component of the core-TFIIHbasal transcription factor, involved in nucleotide excision repair (NER) ofDNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.It acts by opening DNA either around the RNA transcription start site orthe DNA.Eukaryotic ATP-dependent DNA helicase Q. A DNA helicase that may play arole in the repair of DNA that is damaged by ultraviolet light or othermutagens.Bacterial and eukaryotic antiviral SKI2-like helicase. SKI2 has a role inthe 3'-mRNA degradation pathway, repressing dsRNA virus propagation byspecifically blocking translation of viral mRNAs, perhaps recognizing theabsence of CAP or poly(A).Bacterial DNA-damage-inducible protein G (DinG). A probable helicaseinvolved in DNA repair and perhaps also replication [].Bacterial primosomal protein N' (PriA). PriA protein is one of sevenproteins that make up the restart primosome, an apparatus that promotesassembly of replisomes at recombination intermediates and stalledreplication forks.Bacterial ATP-dependent DNA helicase recG. It has a critical role inrecombination and DNA repair, helping process Holliday junctionintermediates to mature products by catalyzing branch migration. It has aDNA unwinding activity characteristic of helicases with a 3' to 5'polarity.A variety of DNA and RNA virus helicases and transcription factorsThis entry represents the ATP-binding domain found within bacterial DinG and eukaryotic Rad3 proteins, differing from other SF1 and SF2 helicases by the presence of a large insert after the Walker A motif [].
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Protein Domain
IPR045028 | DinG/Rad3-like
Type: Family
Description: Helicases have been classified in 5 superfamilies (SF1-SF5). All of the proteins bind ATP and, consequently, all of them carry the classical Walker A(phosphate-binding loop or P-loop) and Walker B(Mg2+-binding aspartic acid) motifs. For the two largest groups, commonlyreferred to as SF1 and SF2, a total of seven characteristic motifs has beenidentified []. These two superfamilies encompass a large number of DNA andRNA helicases from archaea, eubacteria, eukaryotes and viruses that seem to beactive as monomers or dimers. RNA and DNA helicases are considered to beenzymes that catalyze the separation of double-stranded nucleic acids in anenergy-dependent manner [].The various structures of SF1 and SF2 helicases present a common core with twoα-β RecA-like domains [, ]. Thestructural homology with the RecA recombination protein covers the fivecontiguous parallel beta strands and the tandem alpha helices. ATP binds tothe amino proximal α-β domain, where the Walker A (motif I) and WalkerB (motif II) are found. The N-terminal domain also contains motif III (S-A-T)which was proposed to participate in linking ATPase and helicase activities.The carboxy-terminal α-β domain is structurally very similar to theproximal one even though it is bereft of an ATP-binding site, suggesting thatit may have originally arisen through gene duplication of the first one.Some members of helicase superfamilies 1 and 2 are listed below:DEAD-box RNA helicases. The prototype of DEAD-boxproteins is the translation initiation factor eIF4A. The eIF4A protein isan RNA-dependent ATPase which functions together with eIF4B as an RNAhelicase [].DEAH-box RNA helicases. Mainly pre-mRNA-splicing factorATP-dependent RNA helicases [].Eukaryotic DNA repair helicase RAD3/ERCC-2, an ATP-dependent 5'-3' DNAhelicase involved in nucleotide excision repair of UV-damaged DNA.Eukaryotic TFIIH basal transcription factor complex helicase XPB subunit.An ATP-dependent 3'-5' DNA helicase which is a component of the core-TFIIHbasal transcription factor, involved in nucleotide excision repair (NER) ofDNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.It acts by opening DNA either around the RNA transcription start site orthe DNA.Eukaryotic ATP-dependent DNA helicase Q. A DNA helicase that may play arole in the repair of DNA that is damaged by ultraviolet light or othermutagens.Bacterial and eukaryotic antiviral SKI2-like helicase. SKI2 has a role inthe 3'-mRNA degradation pathway, repressing dsRNA virus propagation byspecifically blocking translation of viral mRNAs, perhaps recognizing theabsence of CAP or poly(A).Bacterial DNA-damage-inducible protein G (DinG). A probable helicaseinvolved in DNA repair and perhaps also replication [].Bacterial primosomal protein N' (PriA). PriA protein is one of sevenproteins that make up the restart primosome, an apparatus that promotesassembly of replisomes at recombination intermediates and stalledreplication forks.Bacterial ATP-dependent DNA helicase recG. It has a critical role inrecombination and DNA repair, helping process Holliday junctionintermediates to mature products by catalyzing branch migration. It has aDNA unwinding activity characteristic of helicases with a 3' to 5'polarity.A variety of DNA and RNA virus helicases and transcription factorsThis entry includes bacterial DinG and eukaryotic Rad3 proteins, differing from other SF1 and SF2 helicases by the presence of a large insert after the Walker A motif [].
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Protein
Q8C1K4
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: false
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Protein
Q5SXJ3
Organism: Mus musculus/domesticus
Length: 1174  
Fragment?: false
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Protein
Q3TER9
Organism: Mus musculus/domesticus
Length: 898  
Fragment?: true
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Publication
2546125 | -
First Author: Gorbalenya AE
Year: 1989
Journal: Nucleic Acids Res
Title: Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes.
Volume: 17
Issue: 12
Pages: 4713-30
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Protein
Q6AXC6
Organism: Mus musculus/domesticus
Length: 906  
Fragment?: false
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Protein
Q0VGM9
Organism: Mus musculus/domesticus
Length: 1203  
Fragment?: false
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Protein
A0A286YCB9
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: true
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Protein
A0A2Y9CZM3
Organism: Mus musculus/domesticus
Length: 880  
Fragment?: false
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Protein
A2AU08
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: true
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Protein
A0A286YDY6
Organism: Mus musculus/domesticus
Length: 393  
Fragment?: false
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Protein
Q3TE55
Organism: Mus musculus/domesticus
Length: 824  
Fragment?: true
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Protein
Z4YLW7
Organism: Mus musculus/domesticus
Length: 992  
Fragment?: true
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Protein
Q6P9R1
Organism: Mus musculus/domesticus
Length: 639  
Fragment?: false
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Protein
Q924H9
Organism: Mus musculus/domesticus
Length: 718  
Fragment?: false
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Protein
Q6PFE3
Organism: Mus musculus/domesticus
Length: 886  
Fragment?: false
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Protein
P70270
Organism: Mus musculus/domesticus
Length: 747  
Fragment?: false
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