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Search results 301 to 400 out of 453 for Erf

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Type Details Score
Publication
16407444 | -
First Author: Nakano T
Year: 2006
Journal: Plant Physiol
Title: Genome-wide analysis of the ERF gene family in Arabidopsis and rice.
Volume: 140
Issue: 2
Pages: 411-32
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Publication
11914131 | -
 
First Author: Iyer LM
Year: 2002
Journal: BMC Genomics
Title: Classification and evolutionary history of the single-strand annealing proteins, RecT, Redbeta, ERF and RAD52.
Volume: 3
Pages: 8
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DO Term
DOID:0061012 | craniosynostosis 4
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Publication
23824578 | -
First Author: Janesick A
Year: 2013
Journal: Development
Title: ERF and ETV3L are retinoic acid-inducible repressors required for primary neurogenesis.
Volume: 140
Issue: 15
Pages: 3095-106
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Protein Domain
IPR007499 | ERF_bacteria_virus
Type: Family
Description: The DNA single-strand annealing proteins (SSAPs), such as RecT, Red-beta, ERF and Rad52, function in RecA-dependent and RecA-independent DNA recombination pathways. This family includes proteins related to ERF [].
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Publication
11971137 | -
First Author: Gu YQ
Year: 2002
Journal: Plant Cell
Title: Tomato transcription factors pti4, pti5, and pti6 activate defense responses when expressed in Arabidopsis.
Volume: 14
Issue: 4
Pages: 817-31
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Protein Domain
IPR041247 | Rad52_fam
Type: Family
Description: The DNA single-strand annealing proteins (SSAPs), such as RecT, Red-beta, ERF and Rad52, function in RecA-dependent and RecA-independent DNA recombination pathways. This family includes proteins related to Rad52. These proteins contain two helix-hairpin-helix motifs [].
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Protein Domain
IPR007232 | Rad52_Rad59_Rad22
Type: Family
Description: The DNA single-strand annealing proteins (SSAPs), such as RecT, Red-beta, ERF and Rad52, function in RecA-dependent and RecA-independent DNA recombination pathways. This family includes proteins related to Rad52. These proteins contain two helix-hairpin-helix motifs [].
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Protein Domain
IPR018330 | RecT_fam
Type: Family
Description: The DNA single-strand annealing proteins (SSAPs), such as RecT, Red-beta, ERF and Rad52, function in RecA-dependent and RecA-independent DNA recombination pathways []. This family includes RecT and related proteins.
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Protein Domain
IPR017392 | AP2/ERF-transcript_factor
Type: Family
Description: This entry represents a group of plant AP2/ERF transcription factors, including pathogenesis-related genes transcriptional activator PTI6 []and ethylene-responsive transcription factor ERF []. PTI6 binds to the GCC-box pathogenesis-related promoter element and activates the defense genes of plants [].
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Protein Domain
IPR020298 | Kil_phage_P22-type
Type: Family
Description: The bacteriophage P22 kil gene, like lambda kil, kills the host cell when it is expressed. The two kil genes, although analogous in cell killing and map location, have no sequence homology. The functions of the P22 and lambda kil genes are not known; however, P22 kil is essential for lytic growth in the absence of abc. Gene arf (accessory recombination function, ) is located just upstream from erf and is essential for P22 growth in the absence of kil [].
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Publication
10022817 | J:53214
First Author: Laudet V
Year: 1999
Journal: Oncogene
Title: Molecular phylogeny of the ETS gene family.
Volume: 18
Issue: 6
Pages: 1351-9
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Protein
E0CZA6
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: false
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Protein
P43352
Organism: Mus musculus/domesticus
Length: 420  
Fragment?: false
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Protein
G5E879
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
Q8VEE2
Organism: Mus musculus/domesticus
Length: 427  
Fragment?: false
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Protein
F6W1D5
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: true
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Publication
2738922 | -
First Author: Semerjian AV
Year: 1989
Journal: J Mol Biol
Title: Genetic structure of the bacteriophage P22 PL operon.
Volume: 207
Issue: 1
Pages: 1-13
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Protein Domain
IPR042525 | Rad52_Rad59_Rad22_sf
Type: Homologous_superfamily
Description: The DNA single-strand annealing proteins (SSAPs), such as RecT, Red-beta, ERF and Rad52, function in RecA-dependent and RecA-independent DNA recombination pathways. This superfamily includes proteins related to Rad52. These proteins contain two helix-hairpin-helix motifs [].Rad52 was identified in Saccharomyces cerevisiae (Baker's yeast) as a component of the homologous recombination repair pathway and to play an important role in both meiotic and mitotic recombination. The human protein is highly homologous in both structure and function. Inthe presence of absence of DNA, Rad52 forms ring-shaped oligomers which bind both single and double stranded DNA, stimulating annealing of complimentary DNA strands and promoting ligation of both cohesive and blunt-end fragments. Rad52 may act as a recombination mediator, optimising catalysis of strand exchange by the Rad51 protein.A C-terminal self-association domain has been identified that mediates formation of higher order oligomers of Rad52 rings. Formation of these oligomers may be important for interaction with more than one DNA molecule [].
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Publication
2163347 | J:43939
First Author: Gunther CV
Year: 1990
Journal: Genes Dev
Title: Sequence-specific DNA binding of the proto-oncoprotein ets-1 defines a transcriptional activator sequence within the long terminal repeat of the Moloney murine sarcoma virus.
Volume: 4
Issue: 4
Pages: 667-79
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Publication
8425553 | -
First Author: Wasylyk B
Year: 1993
Journal: Eur J Biochem
Title: The Ets family of transcription factors.
Volume: 211
Issue: 1-2
Pages: 7-18
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Publication
2253872 | -
First Author: Karim FD
Year: 1990
Journal: Genes Dev
Title: The ETS-domain: a new DNA-binding motif that recognizes a purine-rich core DNA sequence.
Volume: 4
Issue: 9
Pages: 1451-3
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Publication
12559563 | -
 
First Author: Oikawa T
Year: 2003
Journal: Gene
Title: Molecular biology of the Ets family of transcription factors.
Volume: 303
Pages: 11-34
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Publication
14693367 | -
 
First Author: Buchwalter G
Year: 2004
Journal: Gene
Title: Ets ternary complex transcription factors.
Volume: 324
Pages: 1-14
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Protein Domain
IPR000418 | Ets_dom
Type: Domain
Description: Transcription factors are protein molecules that bind to specific DNAsequences in the genome, resulting in the induction or inhibition of genetranscription []. The ets oncogene is such a factor, possessing a region of 85-90 amino acids known as the ETS (erythroblast transformation specific) domain [, , ]. This domain is rich inpositively-charged and aromatic residues, and binds to purine-rich segmentsof DNA. The ETS domain has been identified in other transcription factorssuch as PU.1, human erg, human elf-1, human elk-1, GA binding protein, anda number of others [, , ].It is generally localized at the C terminus of the protein,with the exception of ELF-1, ELK-1, ELK-3, ELK-4 and ERF where it is found atthe N terminus.NMR-analysis of the structure of the Ets domains revealed that it contains three α-helices (1-3)and four-stranded β-sheets (1-4) arranged in the order α1-β1-β2-α2-α3-β3-β4 forming awinged helix-turn-helix (wHTH) topology []. The third α-helix isresponsive to contact to the major groove of the DNA. Different members of the Ets family proteinsdisplay distinct DNA binding specificities. The Ets domains and the flanking amino acid sequencesof the proteins influence the binding affinity, and the alteration of asingle amino acid in the Ets domain can change its DNA binding specificities.
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Publication
7773013 | -
First Author: Weigel D
Year: 1995
Journal: Plant Cell
Title: The APETALA2 domain is related to a novel type of DNA binding domain.
Volume: 7
Issue: 4
Pages: 388-9
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Publication
2535512 | -
First Author: Broglie KE
Year: 1989
Journal: Plant Cell
Title: Functional analysis of DNA sequences responsible for ethylene regulation of a bean chitinase gene in transgenic tobacco.
Volume: 1
Issue: 6
Pages: 599-607
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Publication
10715325 | -
First Author: Fujimoto SY
Year: 2000
Journal: Plant Cell
Title: Arabidopsis ethylene-responsive element binding factors act as transcriptional activators or repressors of GCC box-mediated gene expression.
Volume: 12
Issue: 3
Pages: 393-404
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Publication
9756931 | -
First Author: Hao D
Year: 1998
Journal: J Biol Chem
Title: Unique mode of GCC box recognition by the DNA-binding domain of ethylene-responsive element-binding factor (ERF domain) in plant.
Volume: 273
Issue: 41
Pages: 26857-61
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Publication
15319480 | -
First Author: Magnani E
Year: 2004
Journal: Plant Cell
Title: From endonucleases to transcription factors: evolution of the AP2 DNA binding domain in plants.
Volume: 16
Issue: 9
Pages: 2265-77
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Protein
C7U272
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: true
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Publication
12226092 | -
First Author: Lloyd JA
Year: 2002
Journal: J Biol Chem
Title: Correlation of biochemical properties with the oligomeric state of human rad52 protein.
Volume: 277
Issue: 48
Pages: 46172-8
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Protein Domain
IPR036955 | AP2/ERF_dom_sf
Type: Homologous_superfamily
Description: Ethylene is an endogenous plant hormone that influences many aspects of plant growth and development. Some defense related genes that are induced by ethylene contain a cis-regulatory element known as the Ethylene-Responsive Element (ERE) []. Sequence analysis on various ERE regions has identified a short motif rich in G/C nucleotides, the GCC-box, essential for the response to ethylene. This short motif is recognised by a family of transcrition factors, the ERE binding factors (ERF) [].ERF proteins contain a domain of around 60 amino acids which is also found in the APETALA2 (AP2) protein []. This AP2/ERF domain has been shown in various proteins to be necessary and sufficient to bind the GCC-box [].The structure of the AP2/ERF domain in complex with the target DNA has been solved []. The structure resembles that of bacteriophage integrases and the methyl-CpG-binding domain (MBD): a three-stranded β-sheet and an alpha helix almost parallel to the β-sheet. It contacts DNA via Arg and Trp residues located in the β-sheet. Some proteins known to contain an AP2/ERF domain include:Arabidopsis thaliana ERF1 to 6. Tobacco ethylene-responsive element-binding proteins (EREBPs), homologues of ERF proteins. Arabidopsis thaliana AP2 protein. It regulates meristeme identity, floral organ specification and seed coat development. Arabidopsis thaliana C-repeat/dehydration-responsive element (DRE) binding factor 1 (CBF1 or DREB1) and DREB2. They bind a GCC-box-like element found in dehydratation responsive element. Binding to this element mediates cold-inducible transcription. Arabidopsis thaliana and maize abscisic acid (ABA)-insensitive 4 (ABI4) proteins. They bind to a GCC-box-like element found in ABA-responsive genes.Octadecanoid-derivative responsive catharenthus AP2-domain (ORCA2) protein. It binds a GCC-box-like element in the jasmonate responsive element of Str promoter. Tomato Pto-interacting proteins 4 to 6 (Pti4 to Pti6). Pti5 and 6 bind a GCC-box-like element in regulatory regions of various pathogenesis-related (PR) genes. Trichodesmium erythraeum, Tetrahymena thermophila, Enterobacteria phage RB49 and bacteriophage Felix 01 HNH endonucleases. HNH endonucleases are homing endonucleases that move extensively via lateral gene transfer []. This entry represents the AP2/ERF domain superfamily.
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Protein Domain
IPR001471 | AP2/ERF_dom
Type: Domain
Description: Ethylene is an endogenous plant hormone that influences many aspects of plant growth and development. Some defense related genes that are induced by ethylene contain a cis-regulatory element known as the Ethylene-Responsive Element (ERE) []. Sequence analysis on various ERE regions has identified a short motif rich in G/C nucleotides, the GCC-box, essential for the response to ethylene. This short motif is recognised by a family of transcrition factors, the ERE binding factors (ERF) [].ERF proteins contain a domain of around 60 amino acids which is also found in the APETALA2 (AP2) protein []. This AP2/ERF domain has been shown in various proteins to be necessary and sufficient to bind the GCC-box [].The structure of the AP2/ERF domain in complex with the target DNA has been solved []. The structure resembles that of bacteriophage integrases and the methyl-CpG-binding domain (MBD): a three-stranded β-sheet and an alpha helix almost parallel to the β-sheet. It contacts DNA via Arg and Trp residues located in the β-sheet. Some proteins known to contain an AP2/ERF domain include:Arabidopsis thaliana ERF1 to 6. Tobacco ethylene-responsive element-binding proteins (EREBPs), homologues of ERF proteins. Arabidopsis thaliana AP2 protein. It regulates meristeme identity, floral organ specification and seed coat development. Arabidopsis thaliana C-repeat/dehydration-responsive element (DRE) binding factor 1 (CBF1 or DREB1) and DREB2. They bind a GCC-box-like element found in dehydratation responsive element. Binding to this element mediates cold-inducible transcription. Arabidopsis thaliana and maize abscisic acid (ABA)-insensitive 4 (ABI4) proteins. They bind to a GCC-box-like element found in ABA-responsive genes.Octadecanoid-derivative responsive catharenthus AP2-domain (ORCA2) protein. It binds a GCC-box-like element in the jasmonate responsive element of Str promoter. Tomato Pto-interacting proteins 4 to 6 (Pti4 to Pti6). Pti5 and 6 bind a GCC-box-like element in regulatory regions of various pathogenesis-related (PR) genes. Trichodesmium erythraeum, Tetrahymena thermophila, Enterobacteria phage RB49 and bacteriophage Felix 01 HNH endonucleases. HNH endonucleases are homing endonucleases that move extensively via lateral gene transfer []. This entry represents the AP2/ERF domain.
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Publication
9736626 | -
First Author: Allen MD
Year: 1998
Journal: EMBO J
Title: A novel mode of DNA recognition by a beta-sheet revealed by the solution structure of the GCC-box binding domain in complex with DNA.
Volume: 17
Issue: 18
Pages: 5484-96
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Protein
Q8R4Z4
Organism: Mus musculus/domesticus
Length: 513  
Fragment?: false
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Protein
P41969
Organism: Mus musculus/domesticus
Length: 429  
Fragment?: false
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Protein
P41163
Organism: Mus musculus/domesticus
Length: 335  
Fragment?: false
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Protein
P41971
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
Q8QZW2
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
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Protein
P41158
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Protein
Q9CXC9
Organism: Mus musculus/domesticus
Length: 510  
Fragment?: false
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Protein
P28322
Organism: Mus musculus/domesticus
Length: 485  
Fragment?: false
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Protein
P17433
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: false
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Protein
O35906
Organism: Mus musculus/domesticus
Length: 267  
Fragment?: false
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Protein
Q6P3D7
Organism: Mus musculus/domesticus
Length: 242  
Fragment?: false
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Protein
Q8BJR1
Organism: Mus musculus/domesticus
Length: 528  
Fragment?: false
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Protein
C7C6B0
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
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Protein
Q3UZ20
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: true
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Protein
E0CXR7
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: false
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Protein
A2A5C2
Organism: Mus musculus/domesticus
Length: 480  
Fragment?: false
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Protein
Q3UQ47
Organism: Mus musculus/domesticus
Length: 522  
Fragment?: true
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Protein
C7C6B1
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
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Protein
A9L8S9
Organism: Mus musculus/domesticus
Length: 43  
Fragment?: true
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Protein
Q3UZH4
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
D3YYM5
Organism: Mus musculus/domesticus
Length: 167  
Fragment?: true
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Protein
C7C6A8
Organism: Mus musculus/domesticus
Length: 65  
Fragment?: true
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Protein
A0A1B0GXH8
Organism: Mus musculus/domesticus
Length: 306  
Fragment?: true
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Protein
A6MDC6
Organism: Mus musculus/domesticus
Length: 448  
Fragment?: false
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Protein
A2A5C3
Organism: Mus musculus/domesticus
Length: 486  
Fragment?: false
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Protein
C7C6A9
Organism: Mus musculus/domesticus
Length: 125  
Fragment?: true
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Protein
D3YVU8
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: false
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Protein
A0A0X1KG64
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: true
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Protein
Q7TPR9
Organism: Mus musculus/domesticus
Length: 429  
Fragment?: false
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Protein
A9L8S7
Organism: Mus musculus/domesticus
Length: 43  
Fragment?: true
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Protein
G3UVW8
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: false
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Protein
C7C6B2
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: true
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Protein
Q7TMT9
Organism: Mus musculus/domesticus
Length: 319  
Fragment?: false
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Protein
A0A0U1RPG0
Organism: Mus musculus/domesticus
Length: 267  
Fragment?: true
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Protein
Q5EP41
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
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Protein
C7C6B3
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: true
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Protein
C7C6B4
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: true
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Protein
G3UVX2
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
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Protein
Q91W17
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
A0A140LIR9
Organism: Mus musculus/domesticus
Length: 352  
Fragment?: false
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Protein
Q8BN37
Organism: Mus musculus/domesticus
Length: 268  
Fragment?: false
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Protein
A9L8T0
Organism: Mus musculus/domesticus
Length: 44  
Fragment?: true
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Protein
Q3U1H6
Organism: Mus musculus/domesticus
Length: 513  
Fragment?: false
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Protein
B9EIW0
Organism: Mus musculus/domesticus
Length: 267  
Fragment?: false
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Protein
A9L8S8
Organism: Mus musculus/domesticus
Length: 45  
Fragment?: true
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Protein
Q8C6Q0
Organism: Mus musculus/domesticus
Length: 307  
Fragment?: true
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Protein
A0A5F8MPE2
Organism: Mus musculus/domesticus
Length: 356  
Fragment?: false
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Protein
Q6WJ14
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: true
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Protein
Q3U5L4
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: false
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Protein
P81270
Organism: Mus musculus/domesticus
Length: 486  
Fragment?: false
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Protein
Q60775
Organism: Mus musculus/domesticus
Length: 612  
Fragment?: false
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Protein
P41164
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
Q9Z2U4
Organism: Mus musculus/domesticus
Length: 655  
Fragment?: false
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Protein
O70273
Organism: Mus musculus/domesticus
Length: 300  
Fragment?: false
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Protein
P97360
Organism: Mus musculus/domesticus
Length: 485  
Fragment?: false
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Protein
Q8VDK3
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: false
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Protein
Q9JHC9
Organism: Mus musculus/domesticus
Length: 593  
Fragment?: false
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Protein
Q9WTP3
Organism: Mus musculus/domesticus
Length: 325  
Fragment?: false
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Protein
E0CYN8
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
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Protein
Q3V1F7
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: false
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Protein
Q3TVH6
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: false
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Protein
Q8CCR6
Organism: Mus musculus/domesticus
Length: 437  
Fragment?: false
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Protein
Q549J8
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
Q80WR3
Organism: Mus musculus/domesticus
Length: 442  
Fragment?: false
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Protein
Q3V1H4
Organism: Mus musculus/domesticus
Length: 612  
Fragment?: false
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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

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Cambridge CB2 3EH, United Kingdom