T-complex protein 1 subunit beta (CCT2)
The protein contains 535 amino acids for an estimated molecular weight of 57488 Da.
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable). (updated: Sept. 12, 2018)
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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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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Biological Process
'de novo' posttranslational protein folding
Binding of sperm to zona pellucida
Cellular protein metabolic process
Chaperone mediated protein folding independent of cofactor
Chaperone-mediated protein complex assembly
Neutrophil degranulation
Positive regulation of establishment of protein localization to telomere
Positive regulation of protein localization to Cajal body
Positive regulation of telomerase activity
Positive regulation of telomerase RNA localization to Cajal body
Positive regulation of telomere maintenance via telomerase
Protein folding
Protein stabilization
ScaRNA localization to Cajal body
Toxin transport
The reference OMIM entry for this protein is 605139
Chaperonin containing t-complex polypeptide 1, subunit 2; cct2
Chaperonin containing tcp1, subunit 2
Cct-beta; cctb
DESCRIPTION
The chaperonin containing TCP1 (186980) complex (CCT), also called the TCP1 ring complex, consists of 2 back-to-back rings, each containing 8 unique but homologous subunits, such as CCT2. CCT assists the folding of newly translated polypeptide substrates through multiple rounds of ATP-driven release and rebinding of partially folded intermediate forms. Substrates of CCT include the cytoskeletal proteins actin (see 102560) and tubulin (see 191130), as well as alpha-transducin (139330) (Won et al., 1998).CLONING
Cyclin E (CCNE1; 123837), a partner of the cyclin-dependent kinase CDK2 (116953), is implicated in the positive control of the G1/S phase transition. CCNE1 degradation is regulated by ubiquitination and proteasomal action, which occur upon autophosphorylation and activation of the CCNE1-CDK2 complex. Using a yeast-based screen to identify proteins that interact with CCNE1, Won et al. (1998) obtained a cDNA encoding CCT2, which they called CCT-beta.GENE FUNCTION
By mutational analysis, Won et al. (1998) found that CCT is essential for CCNE1 maturation and accumulation.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CCT2 gene to chromosome 12 (TMAP stSG29825). ... More on the omim web site
Oct. 2, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
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 605139 was added.