BAG family molecular chaperone regulator 2 (BAG2)
The protein contains 211 amino acids for an estimated molecular weight of 23772 Da.
Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release (PubMed:24318877, PubMed:9873016). (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.
- 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
Negative regulation of protein binding
Negative regulation of protein ubiquitination
Negative regulation of ubiquitin protein ligase activity
Positive regulation of proteasomal protein catabolic process
Positive regulation of protein processing
Protein folding
Protein metabolic process
Protein stabilization
Regulation of cellular response to heat
The reference OMIM entry for this protein is 603882
Bcl2-associated athanogene 2; bag2
The chaperone activity of Hsp70 (see 140550) family members such as Hsc70 (600816) is regulated by partner proteins that either modulate the peptide-binding cycle or target the actions of these chaperones to specific proteins and subcellular compartments. The Hip protein collaborates with Hsc70/Hsp70 and DNAJ (see 602837) family proteins to stimulate ATP hydrolysis and thus stabilize Hsc70/Hsp70 complexes with substrate polypeptides. BAG1 (601497) competes with Hip for binding to the Hsc70/Hsp70 ATPase domain and promotes substrate release. Using a yeast 2-hybrid screen with the ATPase domain of Hsc70 as bait, Takayama et al. (1999) isolated cDNAs encoding 2 BAG1-like proteins that they named BAG2 and BAG3 (603883). By searching an EST database, they identified partial cDNAs corresponding to 2 additional BAG1 family members, BAG4 (603884) and BAG5 (603885). All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. Takayama et al. (1999) demonstrated that the BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. Surface plasmon resonance and in vitro protein refolding assays revealed that all 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. These authors stated that the functional antagonisms displayed between BAG family proteins and Hip suggest that a proper balance of these 2 types of protein is required for achieving optimal cycles of substrate binding and release required for inducting conformational changes in proteins, with Hip promoting peptide substrate binding by Hsc70/Hsp70 and BAG family proteins promoting dissociation. ... 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 603882 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed