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Search results 201 to 284 out of 284 for Cul3

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 95  
Fragment?: true
Publication
First Author: Inada S
Year: 2004
Journal: Plant Cell
Title: RPT2 is a signal transducer involved in phototropic response and stomatal opening by association with phototropin 1 in Arabidopsis thaliana.
Volume: 16
Issue: 4
Pages: 887-96
Publication
First Author: Haga K
Year: 2005
Journal: Plant Cell
Title: The Rice COLEOPTILE PHOTOTROPISM1 gene encoding an ortholog of Arabidopsis NPH3 is required for phototropism of coleoptiles and lateral translocation of auxin.
Volume: 17
Issue: 1
Pages: 103-15
Publication
First Author: Holland JJ
Year: 2009
Journal: J Exp Bot
Title: Understanding phototropism: from Darwin to today.
Volume: 60
Issue: 7
Pages: 1969-78
Publication
First Author: Roberts D
Year: 2011
Journal: Plant Cell
Title: Modulation of phototropic responsiveness in Arabidopsis through ubiquitination of phototropin 1 by the CUL3-Ring E3 ubiquitin ligase CRL3(NPH3).
Volume: 23
Issue: 10
Pages: 3627-40
Publication
First Author: Motchoulski A
Year: 1999
Journal: Science
Title: Arabidopsis NPH3: A NPH1 photoreceptor-interacting protein essential for phototropism.
Volume: 286
Issue: 5441
Pages: 961-4
Publication
First Author: Pedmale UV
Year: 2007
Journal: J Biol Chem
Title: Regulation of phototropic signaling in Arabidopsis via phosphorylation state changes in the phototropin 1-interacting protein NPH3.
Volume: 282
Issue: 27
Pages: 19992-20001
Publication
First Author: Inoue S
Year: 2008
Journal: Mol Plant
Title: Leaf positioning of Arabidopsis in response to blue light.
Volume: 1
Issue: 1
Pages: 15-26
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
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 315  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 329  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: false
Publication
First Author: Li Y
Year: 2010
Journal: J Biol Chem
Title: Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase.
Volume: 285
Issue: 18
Pages: 13896-906
Publication
First Author: Xu M
Year: 2015
Journal: Oncotarget
Title: Atypical ubiquitin E3 ligase complex Skp1-Pam-Fbxo45 controls the core epithelial-to-mesenchymal transition-inducing transcription factors.
Volume: 6
Issue: 2
Pages: 979-94
Publication
First Author: Sakai T
Year: 2000
Journal: Plant Cell
Title: RPT2. A signal transducer of the phototropic response in Arabidopsis.
Volume: 12
Issue: 2
Pages: 225-36
Publication  
First Author: Marshall J
Year: 2011
Journal: Adv Exp Med Biol
Title: BTB-Kelch proteins and ubiquitination of kainate receptors.
Volume: 717
Pages: 115-25
Publication
First Author: De Guzman RN
Year: 2004
Journal: J Biol Chem
Title: Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites.
Volume: 279
Issue: 4
Pages: 3042-9
Protein
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
Publication
First Author: De Guzman RN
Year: 2000
Journal: J Mol Biol
Title: Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP.
Volume: 303
Issue: 2
Pages: 243-53
Publication
First Author: Freedman SJ
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha.
Volume: 99
Issue: 8
Pages: 5367-72
Publication
First Author: Freedman SJ
Year: 2003
Journal: Nat Struct Biol
Title: Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2.
Volume: 10
Issue: 7
Pages: 504-12
Publication
First Author: De Guzman RN
Year: 2005
Journal: Biochemistry
Title: CBP/p300 TAZ1 domain forms a structured scaffold for ligand binding.
Volume: 44
Issue: 2
Pages: 490-7
Publication
First Author: Robert HS
Year: 2009
Journal: Plant J
Title: BTB and TAZ domain scaffold proteins perform a crucial function in Arabidopsis development.
Volume: 58
Issue: 1
Pages: 109-21
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
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: false
Publication
First Author: Seol JH
Year: 2001
Journal: Nat Cell Biol
Title: Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly.
Volume: 3
Issue: 4
Pages: 384-91
Publication
First Author: Kario E
Year: 2005
Journal: J Biol Chem
Title: Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling.
Volume: 280
Issue: 8
Pages: 7038-48
Protein Domain
Type: Domain
Description: TAZ (Transcription Adaptor putative Zinc finger) domains are zinc-containing domains found in the homologous transcriptional co-activators CREB-binding protein (CBP) and the P300. CBP and P300 are histone acetyltransferases () that catalyse the reversible acetylation of all four histones in nucleosomes, acting to regulate transcription via chromatin remodelling. These large nuclear proteins interact with numerous transcription factors and viral oncoproteins, including p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1, and are involved in cell growth, differentiation and apoptosis []. Both CBP and P300 have two copies of the TAZ domain, one in the N-terminal region, the other in the C-terminal region. The TAZ1 domain of CBP and P300 forms a complex with CITED2 (CBP/P300-interacting transactivator with ED-rich tail), inhibiting the activity of the hypoxia inducible factor (HIF-1alpha) and thereby attenuating the cellular response to low tissue oxygen concentration []. Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and p300 transcriptional coactivators [].Proteins containing this domain also include a group of land-plant specific proteins, know as the BTB/POZ and TAZ domain-containing (BT) protein. The reports of their interaction with CUL3 are contradictory. They are multifunctional scaffold proteins essential for male and female gametophyte development []. The TAZ domain adopts an all-alpha fold with zinc-binding sites in the loops connecting the helices. The TAZ1 domain in P300 and the TAZ2 (CH3) domain in CBP have each been shown to have four amphipathic helices, organised by three zinc-binding clusters with HCCC-type coordination [, , ].Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures andthe number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 714  
Fragment?: false
Publication
First Author: Ponting CP
Year: 1996
Journal: Trends Biochem Sci
Title: ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins.
Volume: 21
Issue: 1
Pages: 11-13
Protein
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 96  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
Publication
First Author: Stemmann O
Year: 1996
Journal: EMBO J
Title: The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution.
Volume: 15
Issue: 14
Pages: 3611-20
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Pseudogene
Type: pseudogene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 597  
Fragment?: false
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 640  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 640  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 640  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1589  
Fragment?: true
Publication
First Author: Stebbins CE
Year: 1999
Journal: Science
Title: Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function.
Volume: 284
Issue: 5413
Pages: 455-61
Protein
Organism: Mus musculus/domesticus
Length: 2412  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2441  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2429  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 2403  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2441  
Fragment?: false
Publication
First Author: Adams J
Year: 2000
Journal: Trends Cell Biol
Title: The kelch repeat superfamily of proteins: propellers of cell function.
Volume: 10
Issue: 1
Pages: 17-24
Publication
First Author: Furukawa M
Year: 2003
Journal: Nat Cell Biol
Title: Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases.
Volume: 5
Issue: 11
Pages: 1001-7
Publication
First Author: Oberg EA
Year: 2012
Journal: J Biol Chem
Title: Selective proteasomal degradation of the B'β subunit of protein phosphatase 2A by the E3 ubiquitin ligase adaptor Kelch-like 15.
Volume: 287
Issue: 52
Pages: 43378-89
Publication
First Author: Stogios PJ
Year: 2004
Journal: Trends Biochem Sci
Title: The BACK domain in BTB-kelch proteins.
Volume: 29
Issue: 12
Pages: 634-7
Publication  
First Author: Dhanoa BS
Year: 2013
Journal: Hum Genomics
Title: Update on the Kelch-like (KLHL) gene family.
Volume: 7
Pages: 13
Publication
First Author: Matthews JM
Year: 2002
Journal: IUBMB Life
Title: Zinc fingers--folds for many occasions.
Volume: 54
Issue: 6
Pages: 351-5
Publication
First Author: Gamsjaeger R
Year: 2007
Journal: Trends Biochem Sci
Title: Sticky fingers: zinc-fingers as protein-recognition motifs.
Volume: 32
Issue: 2
Pages: 63-70
Publication
First Author: Hall TM
Year: 2005
Journal: Curr Opin Struct Biol
Title: Multiple modes of RNA recognition by zinc finger proteins.
Volume: 15
Issue: 3
Pages: 367-73
Publication
First Author: Brown RS
Year: 2005
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: getting a grip on RNA.
Volume: 15
Issue: 1
Pages: 94-8
Publication
First Author: Klug A
Year: 1999
Journal: J Mol Biol
Title: Zinc finger peptides for the regulation of gene expression.
Volume: 293
Issue: 2
Pages: 215-8
Publication
First Author: Laity JH
Year: 2001
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: new insights into structural and functional diversity.
Volume: 11
Issue: 1
Pages: 39-46