Hsp70-binding protein 1 (HSPBP1)
The protein contains 362 amino acids for an estimated molecular weight of 39474 Da.
Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR. (updated: April 1, 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:rs140649061 |
The reference OMIM entry for this protein is 612939
Heat-shock 70-kd protein-binding protein 1; hspbp1
Hspa-binding protein 1
Hsp70-binding protein 1
CLONING
Using the ATPase domain of human HSP70 (see HSPA1A; 140550) as bait in a yeast 2-hybrid screen of a human heart cDNA library, Raynes and Guerriero (1998) cloned HSPBP1. The deduced 459-amino acid protein has a calculated molecular mass of 39.3 kD and contains 6 consecutive glycines near its N terminus. Northern blot analysis detected a 1.7-kb HSPBP1 transcript in all tissues examined, with highest expression in heart and skeletal muscle. Raynes and Guerriero (1998) also identified an HSPBP1 variant that they called HSPBP2, which has 2 polyadenylation signals rather than the single polyadenylation signal of HSPBP1. The deduced HSPBP2 protein is identical to HSPBP1 except that it has 9 consecutive glycines near the N terminus. Using Northern blot analysis, Raynes and Guerriero (2000) found that the expression pattern of Hspbp1 in rat tissues was distinct from that in human. In rat, highest expression was in testis and lowest expression was in heart and skeletal muscle.GENE FUNCTION
Raynes and Guerriero (1998) showed that human HSPBP1 coprecipitated with Hsp70 and Hsc70 (HSPA8; 600816) from bovine heart lysate. Recombinant HSPBP1 inhibited HSP40 (DNAJB1; 604572)-mediated stimulation of HSP70 ATPase activity in a dose-dependent manner, resulting in reduced ability of HSP70 to renature heat-denatured firefly luciferase. HSPBP1 specifically bound the ATPase domain of HSP70 and inhibited ATP binding. Kabani et al. (2002) showed that human HSPBP1 functioned as a nucleotide exchange factor for HSP70, bovine Hsc70, and the yeast HSP70 ortholog Ssa1. HSPBP1 inhibited ATP binding and induced nucleotide dissociation. It inhibited refolding of luciferase by rabbit reticulocyte lysates, which contain factors required for protein refolding. Raynes and Guerriero (2000) showed that the HSPBP1 and HSPBP2 isoforms had comparable inhibitory activities in luciferase refolding by rabbit reticulocyte lysates. Alberti et al. (2004) found that epitope-tagged HSPBP1 immunoprecipitated HSC70 and the HSC70 cochaperone CHIP (STUB1; 607207) from HeLa cell lysates. In the absence of HSC70, HSPBP1 and CHIP bound each other with low affinity. In the presence of ubiquitin-activating and -conjugating enzymes, CHIP mediated ubiquitination of test proteins when bound to HSC70. Addition of HSPBP1 inhibited CHIP-mediated ubiquitination of test proteins as well as CHIP-mediated ubiquitination of HSC70. Complex formation between HSPBP1, HSC70, and CHIP was necessary for HSPBP1 to inhibit CHIP. Alberti et al. (2004) concluded that HSPBP1 regulates CHIP ubiquitin ligase activity.MAPPING
Hartz (2009) mapped the HSPBP1 gene to chromosome 19q13.42 based on an alignment of the HSPBP1 sequence (GenBank GENBANK AF093420) with the genomic sequence (build 36.1). ... 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 612939 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed