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Search results 1201 to 1300 out of 1557 for Tpr

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 832  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 614  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 614  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 748  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 504  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 434  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 450  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 388  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 313  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 446  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 746  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 174  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1242  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1421  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 983  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 427  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 638  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 289  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1302  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1232  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 427  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: false
Publication
First Author: Groves MR
Year: 1999
Journal: Curr Opin Struct Biol
Title: Topological characteristics of helical repeat proteins.
Volume: 9
Issue: 3
Pages: 383-9
Publication
First Author: Andrade MA
Year: 2001
Journal: J Struct Biol
Title: Protein repeats: structures, functions, and evolution.
Volume: 134
Issue: 2-3
Pages: 117-31
Publication
First Author: Han Y
Year: 2020
Journal: Channels (Austin)
Title: The structure and function of TRIP8b, an auxiliary subunit of hyperpolarization-activated cyclic-nucleotide gated channels.
Volume: 14
Issue: 1
Pages: 110-122
Publication
First Author: Stuart MK
Year: 2017
Journal: Monoclon Antib Immunodiagn Immunother
Title: Fine Epitope Mapping of Monoclonal Antibodies to the DNA Repair Protein, RadA.
Volume: 36
Issue: 3
Pages: 83-94
Publication
First Author: Swingle MR
Year: 2004
Journal: J Biol Chem
Title: Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5.
Volume: 279
Issue: 32
Pages: 33992-9
Publication
First Author: Hinds TD Jr
Year: 2008
Journal: Int J Biochem Cell Biol
Title: Protein phosphatase 5.
Volume: 40
Issue: 11
Pages: 2358-62
Publication
First Author: Chinkers M
Year: 2001
Journal: Trends Endocrinol Metab
Title: Protein phosphatase 5 in signal transduction.
Volume: 12
Issue: 1
Pages: 28-32
Publication
First Author: Andreeva AV
Year: 1999
Journal: Cell Signal
Title: RdgC/PP5-related phosphatases: novel components in signal transduction.
Volume: 11
Issue: 8
Pages: 555-62
Publication
First Author: Zhang J
Year: 2005
Journal: Mol Cell Biol
Title: Protein phosphatase 5 is required for ATR-mediated checkpoint activation.
Volume: 25
Issue: 22
Pages: 9910-9
Publication
First Author: Vaughan CK
Year: 2008
Journal: Mol Cell
Title: Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.
Volume: 31
Issue: 6
Pages: 886-95
Protein Domain
Type: Domain
Description: LapB (lipopolysaccharide assembly protein B) contains three major structural motifs: the N-terminal transmembrane helix, several tetratricopeptide repeats (TPR), and a C-terminal rubredoxin metal binding domain. This entry represents the rubredoxin-like metal binding domain. Rubredoxin proteins form small non-heme iron binding sites that use four cysteine residues to coordinate a single metal ion in a tetrahedral environment. Rubredoxins are most commonly found in bacterial systems, but have also been found in eukaryotes. The key features of these rubredoxin-like domains are the extended loops or 'knuckles' and the tetracysteine mode of iron binding. Structural analysis of LapB from Escherichia coli show that the rubredoxin metal binding domain is intimately bound to the TPR motifs and that this association to the TPR motifs is essential to LPS regulation and growth in vivo []. Proteins containing this domain also include RadA. In E. coli, RadA (or Sms) participates in the recombinational repair of radiation-damaged DNA in a process that uses an undamaged DNA strand in one DNA duplex to fill a DNA strand gap in a homologous sister DNA duplex. RadA carries a zinc finger at the N-terminal domain [].
Protein Domain
Type: Domain
Description: Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs [, , , , ]. This entry represents the C-terminal phosphatase domain. Proteins containing this domain also include yeast Ppt1, which is a serine/threonine phosphatase that regulates Hsp90 chaperone by affecting its ATPase and cochaperone binding activitie []. The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of manycellular processes [, ]. PPPs belong to the metallophosphatase (MPP) superfamily.
Publication
First Author: Capetanaki Y
Year: 1990
Journal: Oncogene
Title: Mouse vimentin: structural relationship to fos, jun, CREB and tpr.
Volume: 5
Issue: 5
Pages: 645-55
Publication
First Author: Melo LG
Year: 1999
Journal: Regul Pept
Title: Chronic hypertension in ANP knockout mice: contribution of peripheral resistance.
Volume: 79
Issue: 2-3
Pages: 109-15
Publication
First Author: Chaudhuri M
Year: 2001
Journal: Gene
Title: Cloning and characterization of a novel serine/threonine protein phosphatase type 5 from Trypanosoma brucei.
Volume: 266
Issue: 1-2
Pages: 1-13
Publication
First Author: Odunuga OO
Year: 2003
Journal: J Biol Chem
Title: Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity.
Volume: 278
Issue: 9
Pages: 6896-904
Publication
First Author: Walsh EK
Year: 2004
Journal: Am J Physiol Heart Circ Physiol
Title: Control of myocardial oxygen consumption in transgenic mice overexpressing vascular eNOS.
Volume: 287
Issue: 5
Pages: H2115-21
Publication
First Author: He J
Year: 2013
Journal: Arterioscler Thromb Vasc Biol
Title: Liver kinase B1 is required for thromboxane receptor-dependent nuclear factor-κB activation and inflammatory responses.
Volume: 33
Issue: 6
Pages: 1297-305
Publication
First Author: Wang Y
Year: 2003
Journal: Eur J Neurosci
Title: A hot spot for hotfoot mutations in the gene encoding the delta2 glutamate receptor.
Volume: 17
Issue: 8
Pages: 1581-90
Protein
Organism: Mus musculus/domesticus
Length: 856  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 830  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 815  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 773  
Fragment?: false
Publication
First Author: Saksouk N
Year: 2014
Journal: Mol Cell
Title: Redundant mechanisms to form silent chromatin at pericentromeric regions rely on BEND3 and DNA methylation.
Volume: 56
Issue: 4
Pages: 580-94
Protein
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
Publication
First Author: Lee YT
Year: 2004
Journal: J Biol Chem
Title: Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain.
Volume: 279
Issue: 16
Pages: 16511-7
Publication
First Author: Garcia-Ranea JA
Year: 2002
Journal: FEBS Lett
Title: p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families.
Volume: 529
Issue: 2-3
Pages: 162-7
Publication
First Author: Khan A
Year: 2015
Journal: Proc Natl Acad Sci U S A
Title: BEND3 represses rDNA transcription by stabilizing a NoRC component via USP21 deubiquitinase.
Volume: 112
Issue: 27
Pages: 8338-43
Publication
First Author: Sathyan KM
Year: 2011
Journal: J Cell Sci
Title: A BEN-domain-containing protein associates with heterochromatin and represses transcription.
Volume: 124
Issue: Pt 18
Pages: 3149-63
Publication
First Author: Khan A
Year: 2015
Journal: Transcription
Title: BEND3 mediates transcriptional repression and heterochromatin organization.
Volume: 6
Issue: 5
Pages: 102-5
Publication
First Author: Pitchai GP
Year: 2017
Journal: Nucleic Acids Res
Title: A novel TPR-BEN domain interaction mediates PICH-BEND3 association.
Volume: 45
Issue: 19
Pages: 11413-11424
Protein Domain
Type: Domain
Description: The GGDEF domain, which has been named after the conserved central sequence pattern GG[DE][DE]F is widespread in prokaryotes. It is typically present in multidomain proteins containing regulatory domains of signaling pathways or protein-protein or protein-ligand interaction modules, such as the response regulatory domain, the PAS/PAC domain, the HAMP domain, the GAF domain, the FHA domain or the TPR repeat. However a few single-domain proteins are also known. The GGDEF domain is involved in signal transduction and is likely to catalyze synthesis or hydrolysis of cyclic diguanylate (c-diGMP, bis(3',5')-cyclic diguanylic acid), an effector molecule that consists of two cGMP moieties bound head-to-tail [, , ].Structural studies of PleD from Caulobacter crescentus show that this domain forms a five-stranded beta sheet surrounded by helices, similar to the catalytic core of adenylate cyclase [].
Protein Domain
Type: Domain
Description: The bipartite CS domain, which was named after CHORD-containing proteins and SGT1 [], is a ~100-residue protein-protein interaction module. The CS domain can be found in stand-alone form, as well as fused with other domains, such as CHORD (), SGS (), TPR (), cytochrome b5 () or b5 reductase, in multidomain proteins []. The CS domain has a compact antiparallel β-sandwich fold consisting of seven β-strands [, ]. Some proteins known to contain a CS domain are listed below []: Eukaryotic proteins of the SGT1 family. Eukaryotic Rar1, related to pathogenic resistance in plants, and to development in animals. Eukaryotic nuclear movement protein nudC. Eukaryotic proteins of the p23/wos2 family, which act as co-chaperone. Animal b5+b5R flavo-hemo cytochrome NAD(P)H oxydoreductase type B. Mammalian integrin beta-1-binding protein 2 (melusin).
Protein Domain
Type: Family
Description: BEND3 is a transcriptional repressor that associates with the nucleolar-remodeling complex (NoRC) and is involved in ribosomal DNA (rDNA) silencing []. SUMOylated BEND3 stabilizes the NoRC component Tip5 via USP21 deubiquitinase []. NorC serves as a molecular platform that recruits chromatin modifiers, such as histone deacetylases and histone methyltransferases, leading to deacetylation of histone H4 and trimethylation of H3K9 and H4K20 []. NoRC also targets histone deacetylases and histone methyltransferases to rDNA to establish a heterochromatic state that inhibits transcription activation. Hence, BEND3 and NoRC seem to play a concerted role in the maintenance of heterochromatin architecture [, ].BEND3 has also been shown to mediate Polycomb recruitment in the absence of H3K9Me3 or DNA methylation at the pericentromeric regions []. BEND3 interacts with PICH (ERCC6L), a DNA translocase required for the maintenance of chromosome stability, and stimulates its translocase and ATPase activities. This interaction occurs via an interface between a TPR domain in PICH and a BEN domain in BEND3 [].
Protein
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 777  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1207  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1862  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1207  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false