T-complex protein 1 subunit zeta-2 (CCT6B)
The protein contains 530 amino acids for an estimated molecular weight of 57821 Da.
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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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| Variant | Description |
|---|---|
| dbSNP:rs9635769 | |
| dbSNP:rs2230552 | |
| dbSNP:rs2230553 |
The reference OMIM entry for this protein is 610730
Chaperonin-containing t-complex polypeptide 1, subunit 6b; cct6b
Chaperonin-containing tcp1, subunit 6b
Cct-zeta 2; cctz2
CLONING
Using differential mRNA display to identify testis-specific transcripts, Ozaki et al. (1996) cloned CCT6B, which they called TSA303. The deduced 540-amino acid protein has a calculated molecular mass of 59.5 kD. CCT6B shares 83% amino acid identity with TCP20 (CCT6A; 104613), suggesting it may be a component of a chaperonin complex. Kubota et al. (1997) cloned mouse Cct6b, which they called Cctz2. The deduced protein contains 531 amino acids. Northern blot analysis of mouse tissues detected Cct6b expression only in testis.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CCT6B gene to chromosome 17 (TMAP RH71331). ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 610730 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).