Prefoldin subunit 3 (VBP1)
The protein contains 197 amino acids for an estimated molecular weight of 22658 Da.
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. (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.
- 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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:rs572013 |
Biological Process
'de novo' posttranslational protein folding
Cellular protein metabolic process
Microtubule-based process
Negative regulation of amyloid fibril formation
Protein folding
Tubulin complex assembly
Cellular Component
Cytoplasm
Cytosol
Intracellular membrane-bounded organelle
Nucleus
Polysome
Prefoldin complex
The reference OMIM entry for this protein is 300133
Von hippel-lindau binding protein 1; vbp1
Prefoldin 3; pfdn3
CLONING
Von Hippel-Lindau syndrome (193300) is associated with mutations in the VHL gene (608537), which encodes a tumor suppressor. Using a yeast 2-hybrid assay to screen for proteins that interact with VHL, Tsuchiya et al. (1996) identified B-cell cDNAs encoding a protein they called VBP1 (VHL binding protein-1). By immunoprecipitation studies and Western analysis, the authors demonstrated that VBP1 forms complexes with VHL in vivo. By immunocytolocalization in mammalian cells expressing one or both proteins, Tsuchiya et al. (1996) found that VHL acts as a molecular chaperone that carries VBP1 from perinuclear granules to the nucleus or cytoplasm. Brinke et al. (1996) reported the presence of a novel inversion in the factor VIII (300841) gene in hemophilic monozygotic twins. Brinke et al. (1996) noted that this novel inversion creates 2 hybrid transcription units. One of these is formed by the promoter and first exon of factor VIII and novel sequences. Brinke et al. (1997) determined that these novel sequences were part of the VBP1 gene. Northern blot analysis revealed that VBP1 is ubiquitously expressed as a 1.7-kb mRNA and a much weaker 5.0-kb mRNA. By primer extension analysis, Brinke et al. (1997) found that there are 2 major and 1 minor transcription start sites. Brinke et al. (1997) cloned cDNAs of the mouse VBP1 homolog. The 160-amino acid mouse and human VBP1 protein sequences were identical. Hemberger et al. (1999) used murine Vbp1 cDNA to investigate the expression of the Vbp1 mRNA in the mouse by in situ hybridization and Northern blot analysis. In fetal stages between days 9 and 18 of gestation, Vbp1 was expressed mainly in the central nervous system, retina, and liver. In addition, at day 12, high expression was observed in the labyrinthine region of the placenta. In later stage placentas, Vbp1 expression was, however, considerably reduced. Northern blot analysis of adult mouse tissues showed that Vbp1 was ubiquitously expressed. In situ analysis of several adult tissues showed that in most tissues the transcripts were evenly distributed. In brain, eye, kidney, and intestine, however, Vbp1 was expressed in specific cell types. In cerebellum and various tumors of VHL patients, no consistent differences in VBP1 expression levels could be detected between tumors characteristic of von Hippel-Lindau disease and normal tissue.GENE STRUCTURE
Brinke et al. (1997) determined that the VBP1 gene contains 6 exons and spans at least 30 kb.MAPPING
By analysis of a YAC contig, Brinke et al. (1997) mapped the VBP1 gene to Xq28, 100 to 150 kb distal to the factor VIII gene. Mapping of the murine Vbp1 gene revealed conserved chromosomal localization between mouse and human in a region homologous to human Xq28 (Hemberger et al., 1999).MOLECULAR GENETICS
Clifford et al. (1999) could demonstrate no mutation in VBP1 in 89 sporadic cases of renal cell carcinoma. ... 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
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 300133 was added.