DnaJ homolog subfamily B member 11 (DNAJB11)
The protein contains 358 amino acids for an estimated molecular weight of 40514 Da.
As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins (PubMed:10827079, PubMed:15525676, PubMed:29706351). Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed (PubMed:15525676). May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (PubMed:10827079). It is necessary for maturation and correct trafficking of PKD1 (PubMed:29706351). (updated: Nov. 7, 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.
- 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.
This protein is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs8147 | |
| PKD6 | |
| PKD6 |
Biological Process
Cellular protein metabolic process
Endoplasmic reticulum unfolded protein response
IRE1-mediated unfolded protein response
MRNA modification
Obsolete activation of signaling protein activity involved in unfolded protein response
Positive regulation of ATPase activity
Protein folding
Protein maturation
Cellular Component
Chaperone complex
Endoplasmic reticulum
Endoplasmic reticulum lumen
Membrane
Nucleus
The reference OMIM entry for this protein is 611341
Dnaj/hsp40 homolog, subfamily b, member 11; dnajb11
Human endoplasmic reticulum-associated dnaj; hedj
Dj9
Apobec1-binding protein 2; abbp2
DESCRIPTION
DNAJB11 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus; a glycine/phenylalanine (G/F)-rich region; and a C-terminal cysteine-rich region (Ohtsuka and Hata, 2000).CLONING
By searching EST databases for J domain-containing proteins, Ohtsuka and Hata (2000) identified 10 mouse and human DNAJ homologs, including mouse Dnajb11. The deduced type II transmembrane protein contains 358 amino acids with an N-terminal J domain. Dnajb11 is predicted to have an N-terminal signal peptide. Using database analysis to identify human homologs of a protein involved in Shiga toxin trafficking in monkey kidney cells, followed by PCR of a human skeletal muscle cDNA library, Yu et al. (2000) cloned DNAJB11, which they called HEDJ. Northern blot analysis detected transcripts of 2.2 and 2.0 kb in all tissues examined, with highest expression in pancreas and testis, and weakest expression in thymus and small intestine. Confocal microscopy showed that epitope-tagged DNAJB11 localized to the endoplasmic reticulum (ER). Protease susceptibility, glycosidase treatment, and detergent solubility assays demonstrated that DNAJB11 is luminally oriented and membrane-associated. Using APOBEC1 (600130) as bait in a yeast 2-hybrid analysis of a liver cDNA library, followed by 5-prime RACE, Lau et al. (2001) cloned DNAJB11, which they called ABBP2. The deduced 358-amino acid protein has a calculated molecular mass of 40.5 kD and shares 99% sequence identity with the mouse protein. DNAJB11 contains a conserved J domain, a weak G/F region, and a region that contains 4 cysteines but lacks the zinc finger domain found in some DNAJ proteins. The secondary and tertiary structures of DNAJB11 closely resemble those of HDJ1 (DNAJB1; 604570). Northern blot analysis detected transcripts of 1.5 and 2.0 kb in all tissues examined.GENE FUNCTION
Using in vitro experiments, Yu et al. (2000) demonstrated that the J domain of DNAJB11 interacted with the ER-associated heat-shock protein BIP (HSPA5; 138120) in an ATP-dependent manner and was capable of stimulating its ATPase activity. Lau et al. (2001) showed that DNAJB11 bound to APOBEC1 via its J domain and neighboring G/F domain. Downregulation of DNAJB11 expression in a human hepatocarcinoma cell line inhibited endogenous APOBEC1-mediated apolipoprotein B (APOB; 107730) mRNA editing. Like other HSP40 proteins, DNAJB11 bound to HSP70 (see HSPA1A, 140550) and had ATPase-stimulating activity. APOBEC1-mediated APOB mRNA editing activity of in vitro tissue extracts required the presence of HSP70/DNAJB11. Although exogenously added ATP was not required for editing activity, removal of the endogenous ATP present in these extracts disrupted DNAJB11-HSP70 interaction and completely inhibited editing.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DNAJB11 gene to chromosome 3 (TMAP SHGC-77609). ... More on the omim web site
Nov. 16, 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 611341 was added.