Neuroblastoma-amplified sequence (NBAS)
The protein contains 2371 amino acids for an estimated molecular weight of 268571 Da.
Involved in Golgi-to-endoplasmic reticulum (ER) retrograde transport; the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:19369418). (updated: Nov. 22, 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.
(right-click above to access to more options from the contextual menu)
No binding partner found
Biological Process
Negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Nuclear-transcribed mRNA catabolic process
Protein transport
Retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
The reference OMIM entry for this protein is 608025
Neuroblastoma-amplified sequence; nbas
Neuroblastoma-amplified gene; nag
CLONING
Using 2-dimensional analysis to identify genes coamplified with MYCN (164840) in neuroblastoma cell lines, followed by searching an EST database and RT-PCR of cDNA from neuroblastoma cell lines, Wimmer et al. (1999) cloned NAG. The deduced 1,352-amino acid protein contains a leucine zipper domain and a ribosomal protein S14 (130620) signature domain in its C-terminal half. Northern blot analysis detected a 4.5-kb transcript in neuroblastoma cell lines. RNA dot blot analysis detected expression in all tissues examined, with strongest expression in adult testis, pancreas, pituitary, and adrenal gland, and in fetal heart, kidney, liver, and lung. By long-range PCR and 5-prime and 3-prime RACE, Scott et al. (2003) cloned 2 NAG variants from a neuroblastoma cell line. The shorter cDNA corresponds to the 4.5-kb transcript identified by Wimmer et al. (1999). The longer cDNA represents a 7.3-kb transcript encoding a deduced 2,371-amino acid protein with a novel N-terminal sequence containing an additional leucine zipper motif, 3 putative transmembrane helices, an endoplasmic reticulum signal sequence, and 2 peroxisomal targeting signals. NAG has 2 clusters of nuclear localization signals, one within the N-terminal sequence unique to the longer variant and the other within the common C-terminal sequence. Northern blot analysis detected both transcripts in several neuroblastoma cell lines; the longer transcript was generally more abundant. A database search revealed NAG ESTs in all tissues and tumor types analyzed. NAG shares 83 to 86% identity with orthologous mouse, rat, and bovine proteins. The C-terminal leucine zipper motifs and the ribosomal S14 motif are not conserved in plant and nematode proteins. By immunohistochemical analysis, Maksimova et al. (2010) demonstrated expression of NBAS in the cytoplasm of retinal ganglia cells, with staining of some inner layer cells, whereas the outer layer cells and optic nerve were not stained. NBAS was also expressed in the cytoplasm of squamous epidermal cells and leukocytes.GENE STRUCTURE
Scott et al. (2003) determined that the NAG gene contains 52 exons and spans 420 kb. The 7.3-kb NAG transcript uses all 52 exons, while the 4.5-kb transcript lacks exons 5 through 25 and part of exon 26. The 5-prime flanking region contains a weak TATA box, a CCAAT box, and binding sites for SP1 (189906), OCT1 (164175), and MYC. A CpG island begins at position -187 and extends into intron 1.MAPPING
By FISH, Wimmer et al. (1999) mapped the NBAS gene to chromosome 2p24-p23, distal to the MYCN gene.GENE FUNCTION
By Southern blot analysis, Wimmer et al. (1999) found NAG amplified in 5 of 8 (63%) MYCN-amplified neuroblastoma cell lines and in 9 of 13 (70%) MYCN-amplified neuroblastoma tumors. Tumors that did not show MYCN amplification lacked NAG amplification. Northern blot analysis determined that amplification of the NAG gene correlated with increased NAG expression. Scott et al. (2003) determined that the whole NAG gene was amplified in 1 of 6 (17%) MYCN-amplified cell lines and in 10 of 50 (20%) MYCN-amplified tumors examined. No amplification of NAG was observed in the absence of MYCN amplification in more than 100 tumors studied. A neuroepithelioma cell line overexpressing the related MYC gene (190080), but not MYCN, showed increased NAG expression. Scott et al. (2003) found that coamplification of NAG was associated with low disease stage in MYCN-amplified t ... More on the omim web site
Feb. 10, 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 608025 was added.