Protein mago nashi homolog (MAGOH)
The protein contains 146 amino acids for an estimated molecular weight of 17164 Da.
Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638). Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense-mediated decay (NMD) pathway (PubMed:23917022). The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. (updated: June 5, 2019)
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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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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Biological Process
Gene expression
MRNA 3'-end processing
MRNA export from nucleus
MRNA splicing, via spliceosome
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Regulation of alternative mRNA splicing, via spliceosome
Regulation of translation
RNA export from nucleus
RNA splicing
Termination of RNA polymerase II transcription
Transcription by RNA polymerase II
The reference OMIM entry for this protein is 602603
Mago nashi, drosophila, homolog of; magoh
CLONING
Drosophila that have mutations in their mago nashi (grandchildless) gene have a 'grandchildless' phenotype, a result of producing progeny with defects in germplasm assembly and germline development. Zhao et al. (1998) cloned a cDNA that appears to encode a human homolog of mago nashi (MAGOH) from a human fetal brain cDNA library. The predicted 146-amino acid MAGOH protein is 90% identical to Drosophila mago nashi. Zhao et al. (1998) also identified a cDNA encoding the mouse MAGOH homolog. The predicted mouse and human MAGOH proteins are 100% identical. Northern blot analysis revealed that MAGOH is expressed ubiquitously in adult human tissues. The expression of mouse Magoh in quiescent fibroblasts was induced by serum stimulation.MAPPING
Using radiation hybrid panels, Zhao et al. (1998) mapped the human MAGOH gene to 1p34-p33 and the mouse Magoh gene near position 51 on chromosome 4.GENE FUNCTION
Palacios et al. (2004) demonstrated that the translation initiation factor EIF4A3 (608546) interacts with Barentsz (MLN51; 606504) and is a component of the oskar messenger RNP localization complex. Moreover, EIF4A3 interacts with Mago-Y14 and thus provides the molecular link between Barentsz and the heterodimer. The mammalian Mago (also known as Magoh)-Y14 (605313) heterodimer is a component of the exon junction complex. The exon junction complex is deposited on spliced mRNAs and functions in nonsense-mediated mRNA decay (NMD), a surveillance mechanism that degrades mRNAs with premature translation termination codons. Palacios et al. (2004) showed that both Barentsz and EIF4A3 are essential for NMD in human cells. Thus, Palacios et al. (2004) concluded that they identified EIF4A3 and Barentsz as components of a conserved protein complex that is essential for mRNA localization in flies and NMD in mammals. Oskar mRNA localization at the posterior pole of the Drosophila oocyte is essential for germline and abdomen formation in the future embryo. Y14/RBM8 and MAGOH, human homologs of nuclear shuttling proteins required for oskar mRNA localization, are core components of the exon-exon junction complex (EJC). The EJC is deposited on mRNAs in a splicing-dependent manner, 20 to 24 nucleotides upstream of exon-exon junctions, independent of the RNA sequence. This indicates a possible role of splicing in oskar mRNA localization, challenging the established notion that the oskar 3-prime untranslated region is sufficient for this process. Oskar mRNA localization at the posterior pole of the Drosophila oocyte is essential for germline and abdomen formation in the future embryo. Hachet and Ephrussi (2004) demonstrated that splicing at the first exon-exon junction of oskar RNA is essential for oskar mRNA localization at the posterior pole. They revisited the issue of sufficiency of the oskar 3-prime untranslated region for posterior localization and showed that the localization of unrelated transcripts bearing the oskar 3-prime untranslated region is mediated by endogenous mRNA. Hachet and Ephrussi (2004) concluded that their results reveal an important new function for splicing: regulation of messenger ribonucleoprotein complex assembly and organization for mRNA cytoplasmic localization. ... More on the omim web site
June 7, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
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
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for MAGOH
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 602603 was added.