Nuclear receptor-binding protein (NRBP1)
The protein contains 535 amino acids for an estimated molecular weight of 59845 Da.
May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases. Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication. (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:rs56004639 | |
| an ovarian mucinous carcinoma sample | |
| dbSNP:rs34260196 |
Biological Process
Endoplasmic reticulum to Golgi vesicle-mediated transport
Gene expression
Intracellular signal transduction
Protein phosphorylation
Transcription initiation from RNA polymerase II promoter
The reference OMIM entry for this protein is 606010
Nuclear receptor-binding protein 1; nrbp1
CLONING
Adaptor proteins modulate multiple signaling pathways by regulating the aggregation of other factors into signaling complexes. By a combination of PCR-based homology cloning, 5-prime RACE, and clones obtained from an EST database, Hooper et al. (2000) isolated a novel human cDNA encoding a putative adaptor protein, which they called NRBP. By EST database searching, they also identified mouse and rat homologs of NRBP with 91% and 89% identity, respectively. The deduced 535-amino acid human protein has a molecular mass of 59.8 kD and contains 2 putative nuclear receptor-binding motifs, a putative binding domain for SH2 domain-containing proteins, a kinase-like domain, a bipartite nuclear localization signal, and 3 sequences rich in glutamic acid, serine, proline, and threonine (PEST) residues. Northern blot analysis detected ubiquitous expression of a 2.4-kb NRBP transcript, with highest levels in testis and lowest levels in thymus. Dot-blot analysis showed highest levels in testis and placenta and lowest levels in hippocampus and thymus. NRBP mRNA was also expressed in each of 15 cultured human tumor cell lines examined. Translation of NRBP mRNA in vitro revealed 3 translation products of 60, 51, and 43 kD, suggesting that translation of NRBP may initiate at multiple sites.MAPPING
By fluorescence in situ hybridization, Hooper et al. (2000) mapped the NRBP1 gene to chromosome 2p23. ... 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 606010 was added.