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Search results 1401 to 1500 out of 1546 for Tpr

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 25  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: false
Publication
First Author: Siderovski DP
Year: 1999
Journal: Trends Biochem Sci
Title: The GoLoco motif: a Galphai/o binding motif and potential guanine-nucleotide exchange factor.
Volume: 24
Issue: 9
Pages: 340-1
Publication
First Author: De Vries L
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: Activator of G protein signaling 3 is a guanine dissociation inhibitor for Galpha i subunits.
Volume: 97
Issue: 26
Pages: 14364-9
Publication
First Author: Natochin M
Year: 2000
Journal: J Biol Chem
Title: AGS3 inhibits GDP dissociation from galpha subunits of the Gi family and rhodopsin-dependent activation of transducin.
Volume: 275
Issue: 52
Pages: 40981-5
Publication
First Author: Kimple RJ
Year: 2002
Journal: Nature
Title: Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits.
Volume: 416
Issue: 6883
Pages: 878-81
Publication
First Author: Christianson JC
Year: 2011
Journal: Nat Cell Biol
Title: Defining human ERAD networks through an integrative mapping strategy.
Volume: 14
Issue: 1
Pages: 93-105
Publication
First Author: Ye JZ
Year: 2004
Journal: J Biol Chem
Title: TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres.
Volume: 279
Issue: 45
Pages: 47264-71
Publication
First Author: Ito R
Year: 2001
Journal: Biochem Biophys Res Commun
Title: Temperature-sensitive phenotype of Chinese hamster ovary cells defective in PEX5 gene.
Volume: 288
Issue: 2
Pages: 321-7
Publication
First Author: Ito R
Year: 2005
Journal: J Biochem
Title: Identification of Pex5pM, and retarded maturation of 3-ketoacyl-CoA thiolase and acyl-CoA oxidase in CHO cells expressing mutant Pex5p isoforms.
Volume: 138
Issue: 6
Pages: 781-90
Publication
First Author: Otera H
Year: 2002
Journal: Mol Cell Biol
Title: Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import.
Volume: 22
Issue: 6
Pages: 1639-55
Publication
First Author: Amery L
Year: 2001
Journal: Biochem J
Title: Identification of PEX5p-related novel peroxisome-targeting signal 1 (PTS1)-binding proteins in mammals.
Volume: 357
Issue: Pt 3
Pages: 635-46
Protein Domain
Type: Conserved_site
Description: In heterotrimeric G-protein signalling, cell surface receptors (GPCRs) arecoupled to membrane-associated heterotrimers comprising a GTP-hydrolysing subunit G-alpha and a G-beta/G-gamma dimer. The inactive form contains the alpha subunit bound to GDP and complexes with the beta and gamma subunit. When the ligand is associated to thereceptor, GDP is displaced from G-alpha and GTP is bound. GTP/G-alpha complex dissociates from the trimer and associates to an effector until the intrinsic GTPase activity of G-alpha returns the protein to GDP bound form. Reassociation of GDP bound G-alpha with G-beta/G-gamma dimer terminates the signal. Several mechanisms regulate the signal output at different stage of the G-protein cascade. Two classes of intracellular proteins act as inhibitors of G protein activation: GTPase activating proteins (GAPs), which enhance GTP hydrolysis (see ),and guanine dissociation inhibitors (GDIs), which inhibit GDP dissociation.The GoLoco or G-protein regulatory (GPR) motif found in various G-proteinregulators [, ]acts as a GDI on G-alpha(i) [, ].The crystal structure of the GoLoco motif in complex with G-alpha(i) has been solved []. It consists of three small alpha helices. The highly conserved Asp-Gln-Arg triad within the GoLoco motif participates directly in GDP binding by extending the arginine side chain into the nucleotide binding pocket, highly reminiscent of the catalytic arginine finger employed in GTPase-activating protein (see ). This addition of an arginine in the binding pocket affects the interaction of GDP with G-alpha and therefore is certainly important for the GoLoco GDI activity [].Some proteins known to contain a GoLoco motif are listed below:Mammalian regulators of G-protein signalling 12 and 14 (RGS12 and RGS14), multifaceted signal transduction regulators.Loco, the drosophila RGS12 homologue.Mammalian Purkinje-cell protein-2 (Pcp2). It may function as a cell-type specific modulator for G protein-mediated cell signalling. It is uniquely expressed in cerebellar Purkinje cells and in retinal bipolar neurons.Eukaryotic Rap1GAP. A GTPase activator for the nuclear ras-related regulatory protein RAP-1A.Drosophila protein Rapsynoid (also known as Partner of Inscuteable, Pins) and its mammalian homologues AGS3 and LGN. They form a G-protein regulator family that also contains TPR repeats.
Protein
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: false
Publication  
First Author: López-Doménech G
Year: 2012
Journal: Nat Commun
Title: The Eutherian Armcx genes regulate mitochondrial trafficking in neurons and interact with Miro and Trak2.
Volume: 3
Pages: 814
Publication
First Author: Roux I
Year: 2006
Journal: Cell
Title: Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse.
Volume: 127
Issue: 2
Pages: 277-89
Protein
Organism: Mus musculus/domesticus
Length: 825  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 362  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 332  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 55  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 540  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: false
Publication
First Author: Hao HX
Year: 2009
Journal: Science
Title: SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma.
Volume: 325
Issue: 5944
Pages: 1139-42
Publication
First Author: McNeil MB
Year: 2012
Journal: J Biol Chem
Title: SdhE is a conserved protein required for flavinylation of succinate dehydrogenase in bacteria.
Volume: 287
Issue: 22
Pages: 18418-28
Publication
First Author: Lee SH
Year: 1998
Journal: J Bacteriol
Title: Nucleotide sequence and spatiotemporal expression of the Vibrio cholerae vieSAB genes during infection.
Volume: 180
Issue: 9
Pages: 2298-305
Publication
First Author: Tischler AD
Year: 2002
Journal: J Bacteriol
Title: The Vibrio cholerae vieSAB locus encodes a pathway contributing to cholera toxin production.
Volume: 184
Issue: 15
Pages: 4104-13
Publication
First Author: Ramón NM
Year: 2010
Journal: Mol Biol Cell
Title: Interdependence of the peroxisome-targeting receptors in Arabidopsis thaliana: PEX7 facilitates PEX5 accumulation and import of PTS1 cargo into peroxisomes.
Volume: 21
Issue: 7
Pages: 1263-71
Publication
First Author: Woodward AW
Year: 2005
Journal: Mol Biol Cell
Title: The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5.
Volume: 16
Issue: 2
Pages: 573-83
Protein Domain
Type: Family
Description: Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions []. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk []. These pathways have been adapted to response to a wide variety of stimuli, including nutrients, cellular redox state, changes in osmolarity, quorum signals, antibiotics, and more []. Two-component systems are comprised of a sensor histidine kinase (HK) and its cognate response regulator (RR) []. The HK catalyses its own auto-phosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, which can then effect changes in cellular physiology, often by regulating gene expression. Some HK are bifunctional, catalysing both the phosphorylation and dephosphorylation of their cognate RR. The input stimuli can regulate either the kinase or phosphatase activity of the bifunctional HK.A variant of the two-component system is the phospho-relay system. Here a hybrid HK auto-phosphorylates and then transfers the phosphoryl group to an internal receiver domain, rather than to a separate RR protein. The phosphoryl group is then shuttled to histidine phosphotransferase (HPT) and subsequently to a terminal RR, which can evoke the desired response [, ].This entry represents VieB-type response regulators. In Vibrio, it is part of a signal transduction pathway involved in cholera toxin production [, ].Response regulators of the microbial two-component signal transduction systems typically consist of an N-terminal CheY-like receiver (phosphoacceptor) domain and a C-terminal output (usually DNA-binding) domain. In response to an environmental stimulus, a phosphoryl group is transferred from the His residue of sensor histidine kinase to an Asp residue in the CheY-like receiver domain of the cognate response regulator [, , ]. Phosphorylation of the receiver domain induces conformational changes that activate an associated output domain, which in turn triggers the response. Phosphorylation-induced conformational changes in response regulator molecules have been demonstrated in direct structural studies [].The output domain found in this group is so far unique. In part, it contains a divergent version of TPR repeats.
Publication
First Author: Jia Z
Year: 1997
Journal: Biochem Cell Biol
Title: Protein phosphatases: structures and implications.
Volume: 75
Issue: 1
Pages: 17-26
Protein
Organism: Mus musculus/domesticus
Length: 1291  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1380  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1331  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1372  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1291  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1372  
Fragment?: false
Publication  
First Author: Kirschner LS
Year: 2016
Journal: Mol Cell Endocrinol
Title: Mouse models of thyroid cancer: A 2015 update.
Volume: 421
Pages: 18-27
Protein
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 350  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 331  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
Publication
First Author: Pei J
Year: 2001
Journal: Proteins
Title: GGDEF domain is homologous to adenylyl cyclase.
Volume: 42
Issue: 2
Pages: 210-6
Publication
First Author: Ausmees N
Year: 2001
Journal: FEMS Microbiol Lett
Title: Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity.
Volume: 204
Issue: 1
Pages: 163-7
Publication
First Author: Shirasu K
Year: 1999
Journal: Cell
Title: A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans.
Volume: 99
Issue: 4
Pages: 355-66
Publication  
First Author: Heizmann CW
Year: 2002
Journal: Methods Mol Biol
Title: The multifunctional S100 protein family.
Volume: 172
Pages: 69-80
Protein
Organism: Mus musculus/domesticus
Length: 663  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1215  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1072  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 525  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 729  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 543  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1216  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: false
Publication
First Author: Ponting CP
Year: 1999
Journal: J Mol Med (Berl)
Title: Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins.
Volume: 77
Issue: 10
Pages: 695-8
Publication
First Author: Wu J
Year: 2023
Journal: Blood Adv
Title: EHBP1L1, an apicobasal polarity regulator, is critical for nuclear polarization during enucleation of erythroblasts.
Volume: 7
Issue: 14
Pages: 3382-3394
Publication
First Author: Okazaki N
Year: 2003
Journal: DNA Res
Title: Prediction of the coding sequences of mouse homologues of KIAA gene: III. the complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.
Volume: 10
Issue: 4
Pages: 167-80
Publication
First Author: Sweet SM
Year: 2009
Journal: Mol Cell Proteomics
Title: Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry.
Volume: 8
Issue: 5
Pages: 904-12
Protein
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 411  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 408  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 420  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 405  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 256  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: true
Publication
First Author: Guo A
Year: 2014
Journal: Mol Cell Proteomics
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
Volume: 13
Issue: 1
Pages: 372-87
Protein
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 528  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 547  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1360  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 733  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1299  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1322  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 723  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1324  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 991  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 723  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 803  
Fragment?: false