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IPR004226 is a Tubulin binding cofactor A.
<p>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 [[cite:PUB00077898]].</p> <p>This entry represents tubulin binding cofactor A (TBCA) from animal, plants and fungi. Human TBCA functions as a molecular chaperone for beta-tubulin [[cite:PUB00025558]]. 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 [[cite:PUB00074025]]. 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 [[cite:PUB00077901]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Biological process | Tubulin complex assembly | The aggregation and bonding together of alpha- and beta-tubulin to form a tubulin heterodimer. | ||
| Biological process | Post-chaperonin tubulin folding pathway | Completion of folding of alpha- and beta-tubulin; takes place subsequent to chaperonin-mediated partial folding; mediated by a complex of folding cofactors. | ||
| Molecular function | Beta-tubulin binding | Interacting selectively and non-covalently with the microtubule constituent protein beta-tubulin. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: tubulin-specific chaperone A-like [Cicer arietinum] gi|502099647|ref|XP_004491528.1| | 8 | ||
| – | Tubulin-specific chaperone A; TAIR: AT2G30410.1 tubulin folding cofactor A (KIESEL); Swiss-Prot: sp|O04350|TBCA_ARATH Tubulin-folding cofactor A; TrEMBL-Plants: tr|I3T2X7|I3T2X7_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0021600 | 7 | ||
| – | Tubulin-specific chaperone A; TAIR: AT2G30410.1 tubulin folding cofactor A (KIESEL); Swiss-Prot: sp|O04350|TBCA_ARATH Tubulin-folding cofactor A; TrEMBL-Plants: tr|I3T2X7|I3T2X7_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0021600 | 7 | ||
| – | Tubulin-specific chaperone A; TAIR: AT2G30410.1 tubulin folding cofactor A (KIESEL); Swiss-Prot: sp|O04350|TBCA_ARATH Tubulin-folding cofactor A; TrEMBL-Plants: tr|I3T2X7|I3T2X7_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0021600 | 7 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| SSF46988 | SUPERFAMILY | 1 | 25.00 |