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Search results 601 to 700 out of 1557 for Tpr

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 246  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 195  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 289  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 500  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 43  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 48  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1437  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 238  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 337  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 394  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 38  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 510  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 310  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 53  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 411  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 626  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 90  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 384  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 688  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 293  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 569  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 43  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 36  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 448  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 457  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 972  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 252  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 651  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 399  
Fragment?: false
Publication
First Author: Raudsepp T
Year: 2012
Journal: PLoS Genet
Title: Genome-wide association study implicates testis-sperm specific FKBP6 as a susceptibility locus for impaired acrosome reaction in stallions.
Volume: 8
Issue: 12
Pages: e1003139
Publication
First Author: Munn K
Year: 2000
Journal: Genetics
Title: The shut-down gene of Drosophila melanogaster encodes a novel FK506-binding protein essential for the formation of germline cysts during oogenesis.
Volume: 156
Issue: 1
Pages: 245-56
Publication
First Author: Preall JB
Year: 2012
Journal: RNA
Title: shutdown is a component of the Drosophila piRNA biogenesis machinery.
Volume: 18
Issue: 8
Pages: 1446-57
Protein Domain
Type: Family
Description: This entry includes FKBP6 from mammals and protein shutdown (shu) from flies. FKBP6 is a testis-sperm specific protein that belongs to the immunophilins FKBP family known to be involved in meiosis, calcium homeostasis, clathrin-coated vesicles, and membrane fusions []. FKBP6 contains a PPIase FKBP-type domain and a TPR domain. However, it is inactive as an isomerase and associates with Hsp90 via its TPR domain []. Protein shutdown is essential for the formation of germline cysts during oogenesis []and is a component of the Drosophila piRNA biogenesis machinery [].
Protein Domain
Type: Homologous_superfamily
Description: The tetratrico peptide repeat region (TPR) is a structural motif present in a wide range of proteins [, , ]. It mediates protein-protein interactions and the assembly of multiprotein complexes []. The TPR motif consists of 3-16 tandem-repeats of 34 amino acids residues, although individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms, ranging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes, such as cell cycle regulation, transcriptional control, mitochondrial and peroxisomal protein transport, neurogenesis and protein folding.The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helix-turn-helix arrangement, with adjacent TPR motifs packing in a parallel fashion, resulting in a spiral of repeating anti-parallel α-helices []. The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24 degrees within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A' of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A, and the other surface presents residues from both helices A and B. The domain represented in this superfamily consists of a multi-helical fold comprised of two curved layers of α-helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis []. These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. The TPR is likely to be an ancient repeat, since it is found in eukaryotes, bacteria and archaea, whereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions, and has the ability to acquire multiple functional roles [].
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: Utz PJ
Year: 1998
Journal: J Biol Chem
Title: The 72-kDa component of signal recognition particle is cleaved during apoptosis.
Volume: 273
Issue: 52
Pages: 35362-70
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: 567  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 327  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 626  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 650  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 615  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 567  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 648  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 602  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 625  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
Publication
First Author: Ma Q
Year: 1997
Journal: J Biol Chem
Title: A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin.
Volume: 272
Issue: 14
Pages: 8878-84
Publication
First Author: Sohocki MM
Year: 2001
Journal: Mamm Genome
Title: Comparative analysis of aryl-hydrocarbon receptor interacting protein-like 1 (Aipl1), a gene associated with inherited retinal disease in humans.
Volume: 12
Issue: 7
Pages: 566-8
Publication
First Author: Zhang M
Year: 2005
Journal: Mol Cell
Title: Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.
Volume: 20
Issue: 4
Pages: 525-38
Publication
First Author: Dmitriev RI
Year: 2007
Journal: Biochem Biophys Res Commun
Title: Characterization of hampin/MSL1 as a node in the nuclear interactome.
Volume: 355
Issue: 4
Pages: 1051-7
Publication
First Author: Pan Z
Year: 2013
Journal: J Mol Biol
Title: Structural and biochemical characterization of the interaction between LGN and Frmpd1.
Volume: 425
Issue: 6
Pages: 1039-49
Publication
First Author: Maniam S
Year: 2015
Journal: Cell Death Differ
Title: Cofactor Strap regulates oxidative phosphorylation and mitochondrial p53 activity through ATP synthase.
Volume: 22
Issue: 1
Pages: 156-63
Publication
First Author: White RA
Year: 2005
Journal: Genomics
Title: Positional cloning of the Ttc7 gene required for normal iron homeostasis and mutated in hea and fsn anemia mice.
Volume: 85
Issue: 3
Pages: 330-7
Publication
First Author: Souquet B
Year: 2018
Journal: Cell Rep
Title: Nup133 Is Required for Proper Nuclear Pore Basket Assembly and Dynamics in Embryonic Stem Cells.
Volume: 23
Issue: 8
Pages: 2443-2454
Publication
First Author: Goda T
Year: 2018
Journal: Genes Dev
Title: Calcitonin receptors are ancient modulators for rhythms of preferential temperature in insects and body temperature in mammals.
Volume: 32
Issue: 2
Pages: 140-155
Publication
First Author: Fan S
Year: 2006
Journal: Biochem Biophys Res Commun
Title: Identification of the functional domains of ANT-1, a novel coactivator of the androgen receptor.
Volume: 341
Issue: 1
Pages: 192-201