ATP-binding cassette sub-family E member 1 (ABCE1)
The protein contains 599 amino acids for an estimated molecular weight of 67314 Da.
Cotranslational quality control factor involved in the No-Go Decay (NGD) pathway (PubMed:21448132). Together with PELO and HBS1L, is required for 48S complex formation from 80S ribosomes and dissociation of vacant 80S ribosomes (PubMed:21448132). Together with PELO and HBS1L, recognizes stalled ribosomes and promotes dissociation of elongation complexes assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and to degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway (PubMed:21448132). Plays a role in the regulation of mRNA turnover (By similarity). Plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA (PubMed:29861391). As part of the PINK1-regulated signaling, ubiquitinated by CNOT4 upon mitochondria damage; this modification generates polyubiquitin signals that recruit autophagy receptors to the mitochondrial outer membrane and initiate mitophagy (PubMed:29861391). RNASEL-specific protein inhibitor which antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) to RNASEL (PubMed:9660177). Negative regulator of the anti-viral effect of the interferon-regulated 2-5A/RNASEL pathway (PubMed:9660177, PubMed:9847332, PubMed:11585831).(Microbial infection) May act as a chaperone for post-translational events during HIV-1 capsid assembly.', '(Microbial infection) Plays a role in the down-regulation of the 2-5A/RNASEL pathway during ence (updated: Feb. 10, 2021)
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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| Variant | Description |
|---|---|
| Confirmed at protein level |
Biological Process
Defense response to virus
Negative regulation of catalytic activity
Negative regulation of endoribonuclease activity
Regulation of translation
Regulation of type I interferon-mediated signaling pathway
Response to virus
Ribosomal subunit export from nucleus
RNA catabolic process
Translational initiation
Translational termination
Viral process
The reference OMIM entry for this protein is 601213
Ribonuclease 4 inhibitor; rns4i
Rnase l inhibitor
Atp-binding cassette, subfamily e, member 1; abce1
CLONING
The 2-5A/RNase L system is a main pathway for viral interferon (147660) action and may play a general role in RNA metabolism. In the pathway, IFN stimulation activates 2-5A synthetases which convert ATP into a set of unusual oligomers known as 2-5A; these oligomers in turn activate RNase L (RNase 4; 180435), which leads to inhibition of protein synthesis by cleaving mRNAs at the 3-prime side of UpNp sequences (summary by Bisbal et al., 1995). Bisbal et al. (1995) described the RNase L inhibitor, a potentially important mediator of the 2-5A/RNase L pathway. RNase L inhibitor blocks the activity of ribonuclease L. The authors cloned the human RNase L inhibitor (symbolized RLI by them) from a Daudi cell expression cDNA library using a radiolabeled 2-5ApCp oligomer. The full-length RLI cDNA encodes a predicted 599-amino acid protein which contains 2 repeated ATP/GTP-binding motifs and an internal repeat of 128 amino acids with 53% sequence identity to each other. Northern blots showed 3.5- and 2.8-kb transcripts in HeLa and Daudi cells which differ in their 3-prime untranslated regions. When the mRNA was expressed in reticulocyte extracts Bisbal et al. (1995) showed that both 2-5A binding and nuclease activities of RNase L were abrogated. Furthermore, they found that the inhibition occurred through association of the inhibitor with RNase L and both proteins were coprecipitated with a nuclease-specific monoclonal antibody. Aubry et al. (1996) also cloned the RNS4I gene and found both a 3.8-kb and a 2.4-kb transcript expressed differentially in all tissues examined. Highest expression of the 2.4-kb transcript was found in the testis, while the 3.8-kb transcript was most abundant in ovaries, testis, spleen, and pancreas.MAPPING
Diriong et al. (1996) mapped the gene, symbolized RNS4I, to 4q31 by fluorescence in situ hybridization. Aubry et al. (1996) confirmed the mapping to 4q21 by in situ hybridization. ... More on the omim web site
Feb. 16, 2021: 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 601213 was added.