BAG family molecular chaperone regulator 5 (BAG5)
The protein contains 447 amino acids for an estimated molecular weight of 51200 Da.
Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. (updated: Oct. 25, 2017)
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.
- 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:rs17854644 |
Biological Process
Golgi organization
Negative regulation of neuron projection development
Negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
Negative regulation of proteasomal ubiquitin-dependent protein catabolic process
Negative regulation of protein refolding
Negative regulation of protein ubiquitination
Negative regulation of ubiquitin-protein transferase activity
Neuron death
Protein folding
Protein stabilization
Regulation of cellular response to heat
Regulation of inclusion body assembly
Regulation of ubiquitin-protein transferase activity
Cellular Component
Cytoplasm
Cytosol
Inclusion body
Membrane
Mitochondrion
Nucleus
Perinuclear region of cytoplasm
The reference OMIM entry for this protein is 603885
Bcl2-associated athanogene 5; bag5
BAG1 (601497) binds the ATPase domains of Hsp70 (see 140550) and Hsc70 (600816), modulating their chaperone activity and functioning as a competitive antagonist to the co-chaperone Hip, which stabilizes Hsc70/Hsp70 complexes with substrate polypeptides. See BAG2 (603882). Takayama et al. (1999) identified cDNAs corresponding to BAG5 and 3 other BAG1-like proteins. These authors concluded that interactions with various BAG family proteins allow opportunities for specification and diversification of Hsp70/Hsc70 chaperone functions. Kalia et al. (2004) demonstrated that rat Bag5 directly interacts with Hsp70 and parkin (PARK2; 602544), an E3 ubiquitin ligase that is mutated in a form of early-onset Parkinson disease (600116). Bag5 inhibited both Hsp70-mediated refolding of misfolded proteins and parkin E3 ubiquitin ligase activity, and enhanced the sequestration of parkin in protein aggregates. In rats, overexpression of Bag5 resulted in increased death of dopaminergic neurons compared to controls, whereas overexpression of an inhibitory mutant Bag5 resulted in increased dopaminergic survival. Kalia et al. (2004) concluded that Bag5 is a negative regulator of both Hsp70 and parkin function that sensitizes dopaminergic neurons to injury-induced death and thus promotes neurodegeneration. ... More on the omim web site
Feb. 5, 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
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603885 was added.