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Search results 301 to 400 out of 1552 for Tpr

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Type Details Score
Protein
A2ACP1-2
Organism: Mus musculus/domesticus
Length: 576  
Fragment?: false
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Protein
Q8VD72-2
Organism: Mus musculus/domesticus
Length: 505  
Fragment?: false
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Protein
Q8BG19-3
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
Q8BG19-2
Organism: Mus musculus/domesticus
Length: 607  
Fragment?: false
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Protein
Q692V3-2
Organism: Mus musculus/domesticus
Length: 600  
Fragment?: false
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Protein
Q692V3-4
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
Q692V3-3
Organism: Mus musculus/domesticus
Length: 487  
Fragment?: false
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Protein
Q9CSP9-2
Organism: Mus musculus/domesticus
Length: 438  
Fragment?: false
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Protein
Q9CSP9-3
Organism: Mus musculus/domesticus
Length: 435  
Fragment?: false
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Protein
Q9CSP9-4
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
O88196
Organism: Mus musculus/domesticus
Length: 1979  
Fragment?: false
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Genotype
Genotype
Symbol: Wdr19/Wdr19
Background: involves: FVB/NJ
Zygosity: hm
Has Mutant Allele: true
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Protein Coding Gene
MGI:1918077 | Trak2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2442982 | Rab8b
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Domain
IPR018704 | TPR_21
Type: Domain
Description: This domain resembles a single unit of a TPR repeat.
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GO Term
GO:0044615 | nuclear pore nuclear basket
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Allele
Tg(TG-TPR/NTRK1)#Rstn | MGI:5569754
Name: transgene insertion, Jay Rothstein
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
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Publication
23300914 | -
First Author: Morgan RM
Year: 2012
Journal: PLoS One
Title: Structure of the TPR domain of AIP: lack of client protein interaction with the C-terminal α-7 helix of the TPR domain of AIP is sufficient for pituitary adenoma predisposition.
Volume: 7
Issue: 12
Pages: e53339
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Protein
O70546-2
Organism: Mus musculus/domesticus
Length: 1424  
Fragment?: false
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Protein
O88196-2
Organism: Mus musculus/domesticus
Length: 1978  
Fragment?: false
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Protein
O88196-6
Organism: Mus musculus/domesticus
Length: 1978  
Fragment?: false
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Protein
O88196-5
Organism: Mus musculus/domesticus
Length: 1578  
Fragment?: false
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Protein
O88196-4
Organism: Mus musculus/domesticus
Length: 1938  
Fragment?: false
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Protein
O88196-3
Organism: Mus musculus/domesticus
Length: 1961  
Fragment?: false
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Publication
22074847 | J:180154
First Author: Yuzawa S
Year: 2011
Journal: Proc Natl Acad Sci U S A
Title: Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN).
Volume: 108
Issue: 48
Pages: 19210-5
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Publication
11126359 | J:67120
First Author: Russell JP
Year: 2000
Journal: Oncogene
Title: The TRK-T1 fusion protein induces neoplastic transformation of thyroid epithelium.
Volume: 19
Issue: 50
Pages: 5729-35
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Publication
32868406 | -
 
First Author: Burroughs AM
Year: 2020
Journal: J Bacteriol
Title: Identification of Uncharacterized Components of Prokaryotic Immune Systems and Their Diverse Eukaryotic Reformulations.
Volume: 202
Issue: 24
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Publication
23277548 | -
First Author: Grenha R
Year: 2013
Journal: Proc Natl Acad Sci U S A
Title: Structural basis for the activation mechanism of the PlcR virulence regulator by the quorum-sensing signal peptide PapR.
Volume: 110
Issue: 3
Pages: 1047-52
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Protein Domain
IPR041315 | PlcR_TPR
Type: Repeat
Description: The bacterial PIcR helix-turn-helix transcription factor includes five TPR units of different lengths []. This entry represents the central, medium-sized TPR repeat.
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Protein Coding Gene
MGI:1914345 | Trak1
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
22454401 | J:210503
First Author: Heiliger KJ
Year: 2012
Journal: Endocr Relat Cancer
Title: Novel candidate genes of thyroid tumourigenesis identified in Trk-T1 transgenic mice.
Volume: 19
Issue: 3
Pages: 409-21
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Allele
Aipl1<tm1Mad> | MGI:3524971
Name: aryl hydrocarbon receptor-interacting protein-like 1; targeted mutation 1, Michael A Dyer
Allele Type: Targeted
Attribute String: Null/knockout
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Allele
Fkbp5<Gt(RRC236)Byg> | MGI:3710108
Name: FK506 binding protein 5; gene trap RRC236, BayGenomics
Allele Type: Gene trapped
Attribute String: Null/knockout, Reporter
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Allele
Tg(TG-TPR/NTRK1)5215Rstn | MGI:5569747
Name: transgene insertion 5215, Jay Rothstein
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
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Genotype
Genotype
Symbol: Tg(TG-TPR/NTRK1)#Rstn/?
Background: involves: 129S4/SvJaeSor * C3H * C57BL/6 * C57BL/6J
Zygosity: ot
Has Mutant Allele: true
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GO Term
GO:0160051 | Cyc8(Ssn6)-Tup1 general repressor complex
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Protein Coding Gene
MGI:95813 | Grid2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Domain
IPR026900 | Ttc7A
Type: Family
Description: This entry represents the tetratricopeptide repeat protein 7A. It contains several TPR repeats. Its function is not clear.
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Publication
19261681 | J:210015
First Author: Fedele M
Year: 2009
Journal: Endocr Relat Cancer
Title: Impairment of the p27kip1 function enhances thyroid carcinogenesis in TRK-T1 transgenic mice.
Volume: 16
Issue: 2
Pages: 483-90
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Publication
15582159 | J:94655
First Author: Dyer MA
Year: 2004
Journal: Brain Res Mol Brain Res
Title: Retinal degeneration in Aipl1-deficient mice: a new genetic model of Leber congenital amaurosis.
Volume: 132
Issue: 2
Pages: 208-20
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Publication
19299492 | J:148547
First Author: Tan MH
Year: 2009
Journal: Hum Mol Genet
Title: Gene therapy for retinitis pigmentosa and Leber congenital amaurosis caused by defects in AIPL1: effective rescue of mouse models of partial and complete Aipl1 deficiency using AAV2/2 and AAV2/8 vectors.
Volume: 18
Issue: 12
Pages: 2099-114
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Publication
27527158 | J:325176
 
First Author: Qiu B
Year: 2016
Journal: Int J Mol Sci
Title: The FKBP5 Gene Affects Alcohol Drinking in Knockout Mice and Is Implicated in Alcohol Drinking in Humans.
Volume: 17
Issue: 8
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Publication
30685540 | J:276038
 
First Author: Qiu B
Year: 2019
Journal: Neuroscience
Title: Loss of FKBP5 Affects Neuron Synaptic Plasticity: An Electrophysiology Insight.
Volume: 402
Pages: 23-36
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Publication
38201293 | J:344321
 
First Author: Williams KE
Year: 2023
Journal: Cells
Title: Sex-Specific Impact of Fkbp5 on Hippocampal Response to Acute Alcohol Injection: Involvement in Alterations of Metabolism-Related Pathways.
Volume: 13
Issue: 1
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Publication
28254433 | J:251422
First Author: Zhang L
Year: 2017
Journal: Biochem Biophys Res Commun
Title: Loss of FKBP5 impedes adipocyte differentiation under both normoxia and hypoxic stress.
Volume: 485
Issue: 4
Pages: 761-767
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Publication
27442117 | J:240120
First Author: Stechschulte LA
Year: 2016
Journal: Endocrinology
Title: FKBP51 Null Mice Are Resistant to Diet-Induced Obesity and the PPARγ Agonist Rosiglitazone.
Volume: 157
Issue: 10
Pages: 3888-3900
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Genotype
Genotype
Symbol: Aipl1/Aipl1
Background: involves: 129S7/SvEvBrd
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Aipl1/Aipl1<+>
Background: involves: 129S7/SvEvBrd
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Fkbp5/Fkbp5
Background: involves: 129P2/OlaHsd * C57BL/6
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tg(TG-TPR/NTRK1)5215Rstn/?
Background: involves: C3H * C57BL/6
Zygosity: ot
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Cdkn1b/Cdkn1b Tg(TG-TPR/NTRK1)#Rstn/?
Background: involves: 129S4/SvJaeSor * C3H * C57BL/6 * C57BL/6J
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Cdkn1b/Cdkn1b<+> Tg(TG-TPR/NTRK1)#Rstn/?
Background: involves: 129S4/SvJaeSor * C3H * C57BL/6 * C57BL/6J
Zygosity: cx
Has Mutant Allele: true
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Publication
3821733 | J:8611
First Author: Dean M
Year: 1987
Journal: Mol Cell Biol
Title: Characterization of the rearranged tpr-met oncogene breakpoint.
Volume: 7
Issue: 2
Pages: 921-4
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Protein
E0CXR9
Organism: Mus musculus/domesticus
Length: 88  
Fragment?: true
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Publication
18158900 | -
First Author: Dunleavy EM
Year: 2007
Journal: Mol Cell
Title: A NASP (N1/N2)-related protein, Sim3, binds CENP-A and is required for its deposition at fission yeast centromeres.
Volume: 28
Issue: 6
Pages: 1029-44
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Protein Domain
IPR019544 | Tetratricopeptide_SHNi-TPR_dom
Type: Domain
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. This entry represents SHNi-TPR (Sim3-Hif1-NASP interrupted TPR), a sequence that is an interrupted form of TPR repeat [].
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Allele
Klc1<tm1Gsn> | MGI:2136259
Name: kinesin light chain 1; targeted mutation 1, Lawrence S B Goldstein
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Publication
22228095 | J:181888
First Author: Ashe A
Year: 2012
Journal: Hum Mol Genet
Title: Mutations in mouse Ift144 model the craniofacial, limb and rib defects in skeletal ciliopathies.
Volume: 21
Issue: 8
Pages: 1808-23
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Publication
17142810 | J:120960
First Author: Yong W
Year: 2007
Journal: J Biol Chem
Title: Essential role for Co-chaperone Fkbp52 but not Fkbp51 in androgen receptor-mediated signaling and physiology.
Volume: 282
Issue: 7
Pages: 5026-36
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Allele
Tg(tetO-TPR/MET,-EGFP)12Tcre | MGI:4949465
Name: transgene insertion 12, Tiziana Crepaldi
Allele Type: Transgenic
Attribute String: Inducible, Inserted expressed sequence, Reporter
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Genotype
Genotype
Symbol: Grid2/Grid2
Background: involves: B10.D2/nSnJ
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Fkbp4/Fkbp4 Fkbp5/Fkbp5
Background: involves: 129P2/OlaHsd * 129S/SvEv * C57BL/6
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Fkbp4/Fkbp4 Fkbp5/Fkbp5<+>
Background: involves: 129P2/OlaHsd * 129S/SvEv * C57BL/6
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Wdr19/Wdr19
Background: involves: FVB/NJ
Zygosity: ht
Has Mutant Allele: true
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Protein Domain
IPR019734 | TPR_repeat
Type: Repeat
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.
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Publication
9482716 | -
First Author: Das AK
Year: 1998
Journal: EMBO J
Title: The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.
Volume: 17
Issue: 5
Pages: 1192-9
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Protein
Q6A0D1
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: true
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Protein
Q810V1
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: true
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Protein
A0A0R4J173
Organism: Mus musculus/domesticus
Length: 658  
Fragment?: false
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Publication
27907189 | -
First Author: Talagas A
Year: 2016
Journal: PLoS Pathog
Title: Structural Insights into Streptococcal Competence Regulation by the Cell-to-Cell Communication System ComRS.
Volume: 12
Issue: 12
Pages: e1005980
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Publication
27907154 | -
First Author: Shanker E
Year: 2016
Journal: PLoS Pathog
Title: Pheromone Recognition and Selectivity by ComR Proteins among Streptococcus Species.
Volume: 12
Issue: 12
Pages: e1005979
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Publication
16605243 | -
First Author: Xu Z
Year: 2006
Journal: Biochemistry
Title: Structure and interactions of the helical and U-box domains of CHIP, the C terminus of HSP70 interacting protein.
Volume: 45
Issue: 15
Pages: 4749-59
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Protein Domain
IPR031938 | INSC_LBD
Type: Domain
Description: This is the LGN-binding domain (LBD) of the inscuteable homologue protein. It interacts with the TPR motifs of G-protein-signaling modulator 2 (GPSM2, also known as LGN) and stabilises LGN [].
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Protein Domain
IPR041312 | CHIP_TPR_N
Type: Domain
Description: This is N-terminal tetratricopeptide repeat (TPR) domain found in CHIP, the C terminus of Hsp70 interacting proteins. The TPR domain of CHIP binds directly to EEVD motifs located at the C termini of Hsc/Hsp70 and Hsp90 [].
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Protein Domain
IPR038205 | INSC_LBD_sf
Type: Homologous_superfamily
Description: This is the LGN-binding domain (LBD) of the inscuteable homologue protein. It interacts with the TPR motifs of G-protein-signaling modulator 2 (GPSM2, also known as LGN) and stabilises LGN [].
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Protein Domain
IPR046491 | DUF6584
Type: Family
Description: This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria, mainly Actinobacteria and Firmicutes. Many members are thought to contain TPR regions. There are two conserved motifs, AxRL and LxxY.
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Protein Domain
IPR017560 | Cyt_c_biogenesis_CcmI
Type: Domain
Description: This TPR repeat-containing protein is the CcmI protein (also called CycH) of c-type cytochrome biogenesis. CcmI is thought to act as an apo-cytochrome c chaperone. This entry describes the N-terminal region.
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Protein Domain
IPR013105 | TPR_2
Type: Repeat
Description: The tetratrico peptide repeat (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 [].This repeat includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by .
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Protein Domain
IPR040799 | ComR_TPR
Type: Domain
Description: In Gram-positive bacteria, cell-to-cell communication mainly relies on extracellular signaling peptides. ComR is a member of the RNPP family, which positively controls competence for natural DNA transformation in streptococci. It is directly activated by the binding of its associated pheromone XIP []. The crystal structure analysis of ComR shows that it contains an N-terminal helix-turn-helix (HTH), DNA binding domain (DBD) and a C-terminal tetratricopeptide repeat (TPR) domain. The TPR domain is composed of 11 α-helices forming 5 TPR motifs followed by an additional C-terminal α-helix 16 called CAP. The pheromone XIP binding site is found in the TPR region. Biochemical and mutational analysis indicate that, if the interacting XIP is accepted it can then trigger the conformational change of the TPR domain to open the DBD-TPR interface to allow dimer formation that is required to bind DNA [].
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Protein Domain
IPR001440 | TPR_1
Type: Repeat
Description: The tetratrico peptide repeat (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 thatTPR adopts a helix-turn-helix arrangement, with adjacent TPR motifs packing in a parallelfashion, resulting in a spiral of repeating anti-parallel α-helices []. The two helices are denotedhelix A and helix B. The packing angle between helix A and helix B is ~24 degrees; within asingle TPR and generates a right-handed superhelical shape. Helix A interacts with helix B andwith helix A' of the next TPR. Two protein surfaces are generated: the inner concave surface iscontributed to mainly by residue on helices A, and the other surface presents residues from bothhelices A and B.
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Protein
Q8BGZ4
Organism: Mus musculus/domesticus
Length: 597  
Fragment?: false
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Protein
Q9DAX9
Organism: Mus musculus/domesticus
Length: 585  
Fragment?: false
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Protein
Q64112
Organism: Mus musculus/domesticus
Length: 472  
Fragment?: false
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Protein
Q80UM3
Organism: Mus musculus/domesticus
Length: 865  
Fragment?: false
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Protein
Q9D4C6
Organism: Mus musculus/domesticus
Length: 346  
Fragment?: false
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Protein
Q9EQR6
Organism: Mus musculus/domesticus
Length: 623  
Fragment?: false
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Protein
Q9WVM3
Organism: Mus musculus/domesticus
Length: 565  
Fragment?: false
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Protein
Q8R349
Organism: Mus musculus/domesticus
Length: 620  
Fragment?: false
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Protein
Q64345
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
Q64282
Organism: Mus musculus/domesticus
Length: 463  
Fragment?: false
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Protein
Q9D2X5
Organism: Mus musculus/domesticus
Length: 619  
Fragment?: false
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Protein
Q8BH15
Organism: Mus musculus/domesticus
Length: 744  
Fragment?: false
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Protein
A6H6E9
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: false
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Protein
A0A1L1SS47
Organism: Mus musculus/domesticus
Length: 405  
Fragment?: false
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Protein
Q8BMX6
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: true
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Protein
Q69Z49
Organism: Mus musculus/domesticus
Length: 947  
Fragment?: true
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Protein
Q6GTM0
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
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Protein
B9EJT8
Organism: Mus musculus/domesticus
Length: 334  
Fragment?: false
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Protein
Q3TV33
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
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Protein
Q9CVZ5
Organism: Mus musculus/domesticus
Length: 150  
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.

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