T-complex protein 1 subunit epsilon (CCT5)
The protein contains 541 amino acids for an estimated molecular weight of 59671 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 |
|---|---|
| dbSNP:rs11557652 | |
| HSNSP |
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
Positive regulation of establishment of protein localization to telomere
Positive regulation of protein localization to Cajal body
Positive regulation of telomerase RNA localization to Cajal body
Positive regulation of telomere maintenance via telomerase
Protein folding
Protein stabilization
Response to virus
Toxin transport
The reference OMIM entry for this protein is 256840
Neuropathy, hereditary sensory, with spastic paraplegia, autosomal recessive
A number sign (#) is used with this entry because autosomal recessive sensory neuropathy with spastic paraplegia is caused by mutations in the CCT5 gene (610150).
CLINICAL FEATURES
Cavanagh et al. (1979) described a seemingly unique form of sensory neuropathy with mutilating ulcerations of the hands and feet similar to that described in entry 162400 except for the additional feature of spastic paraplegia. Three of the patients, 2 of whom were thought to be half sibs (different paternity), developed paraplegia in the first 2 years of life; this was associated at an early stage with the clinical features of a peripheral neuropathy. In contrast, the other 2 patients, a brother and sister, demonstrated paraplegia and neuropathy much later, although it was difficult to date the onset precisely. Thomas et al. (1994) described progressive sensory neuropathy in association with spastic paraplegia and a mutilating acropathy of the lower limbs in 5 patients, including 2 pairs of sibs who were the offspring of normal consanguineous parents. Nerve biopsy in 3 of the patients showed an axonopathy with loss of myelinated nerve fibers of all diameters as well as loss of unmyelinated axons. Bouhouche et al. (2006) reported a consanguineous Moroccan family in which 4 sibs had a severe mutilating sensory neuropathy with spastic paraplegia. Age at onset ranged from 1 to 5 years. The clinical features included lower limb spasticity, hyperreflexia with clonus, positive Babinski sign, and subtle distal amyotrophy with normal motor function. Affected members had distal sensory loss for all modalities in the upper and lower limbs, particularly in the feet. Two patients had 'deformities' of the hands and feet, and most had deep perforating ulcers of the extremities. The oldest patient, aged 34, had scars of healed ulcers in the hands and a history of osteomyelitis of the feet leading to amputation of both legs up to his thighs. Although the progression of spasticity was slow, the sensory neuropathy was rapidly progressive and severe. Electrophysiologic studies showed normal or mildly decreased motor nerve conduction velocities consistent with a sensory axonal neuropathy. MRI of 2 patients showed severe atrophy of the spinal cord, and laboratory investigations of 2 patients showed decreased serum apolipoprotein B (APOB; 107730), total cholesterol, and triglycerides.MAPPING
By genomewide analysis of a consanguineous Moroccan family with sensory neuropathy and spastic paraplegia, Bouhouche et al. (2006) identified a candidate disease locus within a 25-cM region on chromosome 5p15.31-p14.1 between markers D5S2054 and D5S648 (maximum lod score of 3.92).MOLECULAR GENETICS
In 4 affected members of a Moroccan family reported by Bouhouche et al. (2006), Bouhouche et al. (2006) identified a homozygous mutation in the CCT5 gene (610150.0001). ... 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 256840 was added.