Type |
Details |
Score |
Gene |
Type: |
gene |
Organism: |
human |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
frog, western clawed |
|
•
•
•
•
•
|
Gene |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
dog, domestic |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chimpanzee |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
cattle |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chicken |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
macaque, rhesus |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Publication |
First Author: |
Chen B |
Year: |
2021 |
Journal: |
Front Immunol |
Title: |
Deficiency of eIF4B Increases Mouse Mortality and Impairs Antiviral Immunity. |
Volume: |
12 |
|
Pages: |
723885 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus caroli |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus pahari |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus spretus |
|
•
•
•
•
•
|
Publication |
First Author: |
Liang R |
Year: |
2021 |
Journal: |
J Cachexia Sarcopenia Muscle |
Title: |
H19X-encoded miR-322(424)/miR-503 regulates muscle mass by targeting translation initiation factors. |
Volume: |
12 |
Issue: |
6 |
Pages: |
2174-2186 |
|
•
•
•
•
•
|
Publication |
First Author: |
Borisova E |
Year: |
2024 |
Journal: |
Nat Commun |
Title: |
Protein translation rate determines neocortical neuron fate. |
Volume: |
15 |
Issue: |
1 |
Pages: |
4879 |
|
•
•
•
•
•
|
Publication |
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 |
|
|
|
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
First Author: |
The Jackson Laboratory |
Year: |
2012 |
Journal: |
MGI Direct Data Submission |
Title: |
Alleles produced for the KOMP project by The Jackson Laboratory |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2002 |
|
Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations for FANTOM2 data |
|
|
|
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
|
|
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
First Author: |
The Gene Ontology Consortium |
Year: |
2014 |
|
Title: |
Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2003 |
|
Title: |
MGI Sequence Curation Reference |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Carninci P |
Year: |
2005 |
Journal: |
Science |
Title: |
The transcriptional landscape of the mammalian genome. |
Volume: |
309 |
Issue: |
5740 |
Pages: |
1559-63 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
First Author: |
Adams DJ |
Year: |
2024 |
Journal: |
Nature |
Title: |
Genetic determinants of micronucleus formation in vivo. |
Volume: |
627 |
Issue: |
8002 |
Pages: |
130-136 |
|
•
•
•
•
•
|
Publication |
First Author: |
MGD Nomenclature Committee |
Year: |
1995 |
|
Title: |
Nomenclature Committee Use |
|
|
|
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
First Author: |
GemPharmatech |
Year: |
2020 |
|
Title: |
GemPharmatech Website. |
|
|
|
|
•
•
•
•
•
|
Publication |
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 |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
UniProt-GOA |
Year: |
2012 |
|
Title: |
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
The Jackson Laboratory Mouse Radiation Hybrid Database |
Year: |
2004 |
Journal: |
Database Release |
Title: |
Mouse T31 Radiation Hybrid Data Load |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
The Gene Ontology Consortium |
Year: |
2010 |
|
Title: |
Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs |
|
|
|
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2002 |
|
Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas |
Year: |
2010 |
|
Title: |
Annotation inferences using phylogenetic trees |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Database and National Center for Biotechnology Information |
Year: |
2000 |
Journal: |
Database Release |
Title: |
Entrez Gene Load |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Allen Institute for Brain Science |
Year: |
2004 |
Journal: |
Allen Institute |
Title: |
Allen Brain Atlas: mouse riboprobes |
|
|
|
|
•
•
•
•
•
|
Publication |
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 |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI) |
Year: |
2010 |
Journal: |
Database Download |
Title: |
Consensus CDS project |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Group |
Year: |
2003 |
Journal: |
Database Procedure |
Title: |
Automatic Encodes (AutoE) Reference |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Bairoch A |
Year: |
1999 |
Journal: |
Database Release |
Title: |
SWISS-PROT Annotated protein sequence database |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
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 |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Allele |
Name: |
eukaryotic translation initiation factor 4B; endonuclease-mediated mutation 1, Shanghai Model Organisms Center |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
Allele |
Name: |
eukaryotic translation initiation factor 4B; endonuclease-mediated mutation 2, Shanghai Model Organisms Center |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, mutant strain, endonuclease-mediated mutation |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
First Author: |
Caruthers JM |
Year: |
2002 |
Journal: |
Curr Opin Struct Biol |
Title: |
Helicase structure and mechanism. |
Volume: |
12 |
Issue: |
1 |
Pages: |
123-33 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
34
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein Domain |
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 |
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 |
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 |
Organism: |
Mus musculus/domesticus |
Length: |
87
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1174
 |
Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
898
 |
Fragment?: |
true |
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Publication |
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 |
Organism: |
Mus musculus/domesticus |
Length: |
906
 |
Fragment?: |
false |
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•
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1203
 |
Fragment?: |
false |
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•
•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
168
 |
Fragment?: |
true |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
880
 |
Fragment?: |
false |
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•
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•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
162
 |
Fragment?: |
true |
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•
•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
393
 |
Fragment?: |
false |
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•
•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
824
 |
Fragment?: |
true |
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•
•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
992
 |
Fragment?: |
true |
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•
•
•
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