T-complex protein 1 subunit alpha (TCP1)
The protein contains 556 amino acids for an estimated molecular weight of 60344 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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| Variant | Description |
|---|---|
| a breast cancer sample |
Biological Process
'de novo' posttranslational protein folding
'de novo' protein folding
Binding of sperm to zona pellucida
Cellular protein metabolic process
Chaperone-mediated protein folding
Interleukin-12-mediated signaling pathway
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
Regulation of macrophage apoptotic process
ScaRNA localization to Cajal body
Toxin transport
Translocation of peptides or proteins into host cell cytoplasm
Tubulin complex assembly
The reference OMIM entry for this protein is 186980
T-complex 1; tcp1
T-complex homolog tcp1
A role in the folding of newly translated proteins in the cytosol has been proposed for t-complex polypeptide-1 (TCP1). Tubulin (e.g., 191110) is a major cytosolic protein whose assembly into microtubules is critical to many cellular processes. Yaffe et al. (1992) examined the biogenesis of alpha- and beta-tubulin in rabbit reticulocyte lysate. They found that newly translated tubulin subunits entered a 900-kD complex which contained as its major constituent a 58-kD protein that crossreacted with a monoclonal antiserum against mouse TCP1. This led them to conclude that TCP1 functions as a cytosolic chaperone in the biosynthesis of tubulin. By use of a cDNA probe for the mouse tcp1 locus, part of the t-complex, Willison et al. (1985) assigned the homologous locus to chromosome 6. The finding was confirmed by means of a cDNA probe for the human TCP1 gene. Suspicion that some human malformations are the result of mutation in the t-complex loci is discussed elsewhere (182940). TCP1 codes for a protein which is abundantly expressed in testes as well as in other tissues. Using the cloned gene and a panel of somatic cell hybrids, as well as in situ hybridization, Willison et al. (1987) assigned the gene to 6q23-qter; thus, it is not closely linked to the HLA complex. For this reason and others, TCP1 is not likely to be a human equivalent of the mouse t-complex. Blanche et al. (1987) found that TCP1 is not linked to HLA and GLO1 and is probably excluded from 6p. This result was consistent with the reported localization to 6q23-qter. By in situ hybridization, Fonatsch et al. (1987) concluded that the TCP1 locus is probably in the 6q25-q27 region. Blanche et al. (1992) demonstrated that the TCP1 and plasminogen (173350) genes show no recombination and are located about 50 cM proximal to TCP10 (187020), which is located in band 6q27. The ACAT2 gene (100678) shows complementary overlapping with the 3-prime region of the TCP1 gene in both mouse and human. These genes are encoded on opposite strands of DNA, as well as in opposite transcriptional orientation. Masuno et al. (1996) assigned the ACAT2 gene to 6q25.3-q26 by fluorescence in situ hybridization; thus the assignment of the TCP1 gene can be refined to 6q25.3-q26. ... 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 186980 was added.