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Search results 101 to 163 out of 163 for Tbcb

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Type Details Score
Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
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Publication
- | J:155845
     
First Author: Wellcome Trust Sanger Institute
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Wellcome Trust Sanger Institute
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Publication
- | J:238766
     
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
18799693 | J:142754
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
25908846 | -
First Author: Serna M
Year: 2015
Journal: J Cell Sci
Title: The structure of the complex between α-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism.
Volume: 128
Issue: 9
Pages: 1824-34
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Publication
23627368 | -
First Author: Fleming JR
Year: 2013
Journal: FEBS J
Title: The architecture of Trypanosoma brucei tubulin-binding cofactor B and implications for function.
Volume: 280
Issue: 14
Pages: 3270-80
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Protein Domain
IPR045172 | TBCB_N_Ubl
Type: Domain
Description: Tubulin-folding cofactor B (TBCB) is one of protein cofactors A through E that is required for the folding of tubulins prior to their incorporation into microtubules and heterodimer assembly. TBCB comprises an N-terminal ubiquitin-like (Ubl) domain and a C-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain. The Ubl domain of TBCB is essential for proper folding and assembly of tubulin alpha. It has a β-grasp Ubl fold, a common structure involved in protein-protein interactions. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. TBC-A through E are necessary for the biogenesis of microtubules and for cell viability [, ].
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Publication
16303566 | J:103926
First Author: Wang W
Year: 2005
Journal: Curr Biol
Title: Gigaxonin interacts with tubulin folding cofactor B and controls its degradation through the ubiquitin-proteasome pathway.
Volume: 15
Issue: 22
Pages: 2050-5
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Protein
P48428
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
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Protein
A0A1Y7VJ48
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: false
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Protein
Q5I0U7
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
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Publication
12054808 | J:76643
First Author: Guasch A
Year: 2002
Journal: J Mol Biol
Title: Three-dimensional structure of human tubulin chaperone cofactor A.
Volume: 318
Issue: 4
Pages: 1139-49
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Publication
11739729 | -
First Author: Abruzzi KC
Year: 2002
Journal: Mol Cell Biol
Title: Protection from free beta-tubulin by the beta-tubulin binding protein Rbl2p.
Volume: 22
Issue: 1
Pages: 138-47
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Publication
15321725 | -
First Author: You L
Year: 2004
Journal: J Mol Biol
Title: Model for the yeast cofactor A-beta-tubulin complex based on computational docking and mutagensis.
Volume: 341
Issue: 5
Pages: 1343-54
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Protein
B1ATU0
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: true
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Protein
F6UI15
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: true
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Publication
23973072 | -
 
First Author: Tian G
Year: 2013
Journal: Methods Cell Biol
Title: Tubulin-specific chaperones: components of a molecular machine that assembles the α/β heterodimer.
Volume: 115
Pages: 155-71
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Publication
12225668 | -
First Author: Kirik V
Year: 2002
Journal: Curr Biol
Title: Functional analysis of the tubulin-folding cofactor C in Arabidopsis thaliana.
Volume: 12
Issue: 17
Pages: 1519-23
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Publication
11847227 | -
First Author: Bartolini F
Year: 2002
Journal: J Biol Chem
Title: Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C.
Volume: 277
Issue: 17
Pages: 14629-34
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Publication
11959844 | -
First Author: Steinborn K
Year: 2002
Journal: Genes Dev
Title: The Arabidopsis PILZ group genes encode tubulin-folding cofactor orthologs required for cell division but not cell growth.
Volume: 16
Issue: 8
Pages: 959-71
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Publication
10099932 | -
First Author: Mayer U
Year: 1999
Journal: Eur J Cell Biol
Title: Mutations in the pilz group genes disrupt the microtubule cytoskeleton and uncouple cell cycle progression from cell division in Arabidopsis embryo and endosperm.
Volume: 78
Issue: 2
Pages: 100-8
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Publication
26208336 | -
   
First Author: Nithianantham S
Year: 2015
Journal: Elife
Title: Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamics.
Volume: 4
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Protein Domain
IPR004226 | TBCA
Type: Family
Description: The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin polypeptides (via multiple rounds of ATP-dependent interaction with the cytosolic chaperonin), TBCA and TBCB bind to and stabilise newly synthesised beta- and alpha-tubulin, respectively. The exchange of beta-tubulin between TBCA and TBCD, and of alpha-tubulin between TBCB and TBCE, resulting in the formation of TBCD/beta and TBCE/alpha. These two complexes then interact with each other and form a supercomplex (TBCE/alpha/TBCD/beta). Interaction of the supercomplex with TBCC causes the disassembly of the supercomplex and the release of E-site GDP-bound alpha/beta tubulin heterodimer, which becomes polymerization competent following spontaneous exchange with GTP [].This entry represents tubulin binding cofactor A (TBCA) from animal, plants and fungi. Human TBCA functions as a molecular chaperone for beta-tubulin []. Budding yeast TBCA, also known as Rbl2, may bind transiently to free beta-tubulin, which then passes into an aggregated form that is not toxic []. The sequence identity of Rbl2 and human TBCA is only 32%, they appear to be structurally distinct and may interact with beta-tubulin by different mechanisms [].
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Protein Domain
IPR036126 | TBCA_sf
Type: Homologous_superfamily
Description: The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin polypeptides (via multiple rounds of ATP-dependent interaction with the cytosolic chaperonin), TBCA and TBCB bind to and stabilise newly synthesised beta- and alpha-tubulin, respectively. The exchange of beta-tubulin between TBCA and TBCD, and of alpha-tubulin between TBCB and TBCE, resulting in the formation of TBCD/beta and TBCE/alpha. These two complexes then interact with each other and form a supercomplex (TBCE/alpha/TBCD/beta). Interaction of the supercomplex with TBCC causes the disassembly of the supercomplex and the release of E-site GDP-bound alpha/beta tubulin heterodimer, which becomes polymerization competent following spontaneous exchange with GTP [].This entry represents tubulin binding cofactor A (TBCA) from animal, plants and fungi. Human TBCA functions as a molecular chaperone for beta-tubulin []. Budding yeast TBCA, also known as Rbl2, may bind transiently to free beta-tubulin, which then passes into an aggregated form that is not toxic []. The sequence identity of Rbl2 and human TBCA is only 32%, they appear to be structurally distinct and may interact with beta-tubulin by different mechanisms []. The structure of TBCA has three helices forming a bundle closed fold with left-handed twist topology going up-and-down.
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Protein Domain
IPR027684 | TBCC
Type: Family
Description: The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin polypeptides (via multiple rounds of ATP-dependent interaction with the cytosolic chaperonin), TBCA and TBCB bind to and stabilise newly synthesised beta- and alpha-tubulin, respectively. The exchange of beta-tubulin between TBCA and TBCD, and of alpha-tubulin between TBCB and TBCE, resulting in the formation of TBCD/beta and TBCE/alpha. These two complexes then interact with each other and form a supercomplex (TBCE/alpha/TBCD/beta). Interaction of the supercomplex with TBCC causes the disassembly of the supercomplex and the release of E-site GDP-bound alpha/beta tubulin heterodimer, which becomes polymerization competent following spontaneous exchange with GTP [].This entry represents tubulin-specific chaperone C (TBCC, also known as tubulin-folding cofactor C), which is involved in the final step of the tubulin folding pathway [, ]. In Arabidopsis thaliana, it is required for continuous microtubule cytoskeleton organisation, mitotic division, cytokinesis, and to couple cell cycle progression to cell division in embryos and endosperms [, ].
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Protein Domain
IPR033162 | TBCD
Type: Family
Description: The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin polypeptides (via multiple rounds of ATP-dependent interaction with the cytosolic chaperonin), TBCA and TBCB bind to and stabilise newly synthesised beta- and alpha-tubulin, respectively. The exchange of beta-tubulin between TBCA and TBCD, and of alpha-tubulin between TBCB and TBCE, resulting in the formation of TBCD/beta and TBCE/alpha. These two complexes then interact with each other and form a supercomplex (TBCE/alpha/TBCD/beta). Interaction of the supercomplex with TBCC causes the disassembly of the supercomplex and the release of E-site GDP-bound alpha/beta tubulin heterodimer, which becomes polymerization competent following spontaneous exchange with GTP [].This entry represents tubulin-folding cofactor D (TBCD) and its homologues. Its ability to interact with beta tubulin is regulated via its interaction with ARL2 (ADP ribosylation factor-like protein 2), a small monomeric G protein. ARL2 inhibits the beta-tubulin GTPase activating protein (GAP) activity of TBCD, and its interaction with native tubulin dimers [, ].
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Protein
Q8CHC0
Organism: Mus musculus/domesticus
Length: 352  
Fragment?: true
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Protein
Q8R199
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: true
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Publication
15364906 | -
First Author: Lytle BL
Year: 2004
Journal: J Biol Chem
Title: Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B.
Volume: 279
Issue: 45
Pages: 46787-93
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Publication
10831612 | -
First Author: Bhamidipati A
Year: 2000
Journal: J Cell Biol
Title: ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin.
Volume: 149
Issue: 5
Pages: 1087-96
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Protein
Q9D1E6
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: false
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Protein
Q8BYA0
Organism: Mus musculus/domesticus
Length: 1196  
Fragment?: false
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Protein
Q8VCN9
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false
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Protein
A0A0R4J0M1
Organism: Mus musculus/domesticus
Length: 341  
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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