| Type |
Details |
Score |
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
84
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
72
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
|
|
•
•
•
•
•
|
| Protein Domain |
| 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 []. |
|
•
•
•
•
•
|
| Protein Domain |
| 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. |
|
•
•
•
•
•
|
| Protein Domain |
| 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 [, ]. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
352
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
151
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1196
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
347
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dickinson ME |
| Year: |
2016 |
| Journal: |
Nature |
| Title: |
High-throughput discovery of novel developmental phenotypes. |
| Volume: |
537 |
| Issue: |
7621 |
| Pages: |
508-514 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
International Knockout Mouse Consortium |
| Year: |
2014 |
| Journal: |
Database Download |
| Title: |
MGI download of modified allele data from IKMC and creation of new knockout alleles |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
International Mouse Strain Resource |
| Year: |
2014 |
| Journal: |
Database Download |
| Title: |
MGI download of germline transmission data for alleles from IMSR strain data |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ko MS |
| Year: |
2000 |
| Journal: |
Development |
| Title: |
Large-scale cDNA analysis reveals phased gene expression patterns during preimplantation mouse development. |
| Volume: |
127 |
| Issue: |
8 |
| Pages: |
1737-49 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2002 |
|
| Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations for FANTOM2 data |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Helmholtz Zentrum Muenchen GmbH |
| Year: |
2010 |
| Journal: |
MGI Direct Data Submission |
| Title: |
Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu) |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cyagen Biosciences Inc. |
| Year: |
2022 |
|
| Title: |
Cyagen Biosciences Website. |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2002 |
|
| Title: |
Function or Process or Component Unknown following Literature Review |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
GemPharmatech |
| Year: |
2020 |
|
| Title: |
GemPharmatech Website. |
|
|
|
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
UniProt-GOA |
| Year: |
2012 |
|
| Title: |
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2003 |
|
| Title: |
MGI Sequence Curation Reference |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2002 |
|
| Title: |
Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gerhard DS |
| Year: |
2004 |
| Journal: |
Genome Res |
| Title: |
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |
| Volume: |
14 |
| Issue: |
10B |
| Pages: |
2121-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
MGD Nomenclature Committee |
| Year: |
1995 |
|
| Title: |
Nomenclature Committee Use |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
The Jackson Laboratory Mouse Radiation Hybrid Database |
| Year: |
2004 |
| Journal: |
Database Release |
| Title: |
Mouse T31 Radiation Hybrid Data Load |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Church DM |
| Year: |
2009 |
| Journal: |
PLoS Biol |
| Title: |
Lineage-specific biology revealed by a finished genome assembly of the mouse. |
| Volume: |
7 |
| Issue: |
5 |
| Pages: |
e1000112 |
|
•
•
•
•
•
|