Tubulin-specific chaperone A (TBCA)
The protein contains 108 amino acids for an estimated molecular weight of 12855 Da.
Tubulin-folding protein; involved in the early step of the tubulin folding pathway. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
'de novo' posttranslational protein folding
Cellular protein metabolic process
Post-chaperonin tubulin folding pathway
Protein folding
Tubulin complex assembly
Cellular Component
Cytoplasm
Cytosol
Extracellular exosome
Microtubule
Microtubule cytoskeleton
Nucleolus
Molecular Function
Beta-tubulin binding
Chaperone binding
Poly(A) RNA binding
RNA binding
Tubulin binding
The reference OMIM entry for this protein is 610058
Tubulin-specific chaperone a; tbca
Chaperonin cofactor a
DESCRIPTION
Microtubules are polymers of alpha-tubulin (see TUBA1; 191110) and beta-tubulin (see TUBB; 191130) that participate in essential cell functions. A multistep process involving molecular chaperones and cofactors, including TBCA, produces tubulin heterodimers competent to polymerize. TBCA specifically interacts with a folding intermediate of beta-tubulin and acts as a molecular chaperone (Nolasco et al., 2005).CLONING
By sequencing cDNAs obtained from umbilical cord blood CD34 (142230)-positive hematopoietic stem/progenitor cells, Mao et al. (1998) identified TBCA.GENE FUNCTION
Tian et al. (1996) found that purified bovine cofactor A formed a stable complex with beta-tubulin intermediates generated by ATP-dependent action of the cytosolic chaperonin complex. Through this interaction, cofactor A appeared to increase the rate of tubulin cycling and, secondarily, to stimulate the ATPase activity of the complex. Using small interfering RNA to silence TBCA expression in HeLa and MCF7 mammary carcinoma cell lines, Nolasco et al. (2005) found that TBCA was essential for cell viability. TBCA knockdown produced a decrease in the amount of soluble tubulin, modifications in microtubules, and G1 cell cycle arrest. In MCF7 cells, cell death was preceded by a change in cell shape resembling differentiation.MAPPING
The International Radiation Hybrid mapping Consortium mapped the TBCA gene to chromosome 5 (TMAP SHGC-34767). ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 610058 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed