| UniProt ID | RBM8A_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y5S9 | |
| Protein Name | RNA-binding protein 8A | |
| Gene Name | RBM8A | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 174 | |
| Subcellular Localization | Nucleus . Nucleus speckle . Cytoplasm . Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear spe | |
| Protein Description | Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. 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. Its removal from cytoplasmic mRNAs requires translation initiation from EJC-bearing spliced mRNAs. Associates preferentially with mRNAs produced by splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. The MAGOH-RBM8A heterodimer is a component of the nonsense mediated decay (NMD) pathway. 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.. | |
| Protein Sequence | MADVLDLHEAGGEDFAMDEDGDESIHKLKEKAKKRKGRGFGSEEGSRARMREDYDSVEQDGDEPGPQRSVEGWILFVTGVHEEATEEDIHDKFAEYGEIKNIHLNLDRRTGYLKGYTLVEYETYKEAQAAMEGLNGQDLMGQPISVDWCFVRGPPKGKRRGGRRRSRSPDRRRR | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MADVLDLHE ------CCCCCCHHH | 18.67 | 21406692 | |
| 24 | Phosphorylation | MDEDGDESIHKLKEK CCCCCCHHHHHHHHH | 34.43 | 29255136 | |
| 27 | Acetylation | DGDESIHKLKEKAKK CCCHHHHHHHHHHHH | 60.63 | 23954790 | |
| 27 | Sumoylation | DGDESIHKLKEKAKK CCCHHHHHHHHHHHH | 60.63 | - | |
| 27 | Sumoylation | DGDESIHKLKEKAKK CCCHHHHHHHHHHHH | 60.63 | 28112733 | |
| 38 | Methylation | KAKKRKGRGFGSEEG HHHHHCCCCCCCHHH | 40.06 | 80701329 | |
| 42 | Phosphorylation | RKGRGFGSEEGSRAR HCCCCCCCHHHHHHH | 30.16 | 29255136 | |
| 42 (in isoform 2) | Phosphorylation | - | 30.16 | 21815630 | |
| 45 (in isoform 2) | Phosphorylation | - | 20.55 | 24719451 | |
| 46 | Phosphorylation | GFGSEEGSRARMRED CCCCHHHHHHHHHHC | 26.50 | 30266825 | |
| 50 | Sulfoxidation | EEGSRARMREDYDSV HHHHHHHHHHCHHHC | 5.55 | 21406390 | |
| 53 (in isoform 2) | Phosphorylation | - | 42.02 | 27762562 | |
| 54 | Phosphorylation | RARMREDYDSVEQDG HHHHHHCHHHCCCCC | 12.83 | 29255136 | |
| 55 (in isoform 2) | Phosphorylation | - | 59.54 | 27762562 | |
| 56 | Phosphorylation | RMREDYDSVEQDGDE HHHHCHHHCCCCCCC | 22.71 | 29255136 | |
| 69 | Phosphorylation | DEPGPQRSVEGWILF CCCCCCCCEEEEEEE | 21.19 | 28348404 | |
| 100 | Ubiquitination | FAEYGEIKNIHLNLD HHHHCCEEEEEEEEC | 45.61 | - | |
| 110 | Phosphorylation | HLNLDRRTGYLKGYT EEEECCCCCCCCCEE | 30.95 | 21601212 | |
| 116 | Phosphorylation | RTGYLKGYTLVEYET CCCCCCCEEEEEEEH | 8.70 | - | |
| 117 | Phosphorylation | TGYLKGYTLVEYETY CCCCCCEEEEEEEHH | 32.75 | 21601212 | |
| 121 | Phosphorylation | KGYTLVEYETYKEAQ CCEEEEEEEHHHHHH | 13.19 | 28152594 | |
| 123 | Phosphorylation | YTLVEYETYKEAQAA EEEEEEEHHHHHHHH | 38.70 | 28152594 | |
| 124 | Phosphorylation | TLVEYETYKEAQAAM EEEEEEHHHHHHHHH | 8.56 | 28152594 | |
| 125 | Ubiquitination | LVEYETYKEAQAAME EEEEEHHHHHHHHHC | 54.73 | - | |
| 166 | Phosphorylation | RRGGRRRSRSPDRRR CCCCCCCCCCCCCCC | 34.99 | 26329039 | |
| 168 | Phosphorylation | GGRRRSRSPDRRRR- CCCCCCCCCCCCCC- | 32.19 | 26329039 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RBM8A_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of RBM8A_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-56, AND MASSSPECTROMETRY. | |
| "A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-166 AND SER-168,AND MASS SPECTROMETRY. | |
| "Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY. | |
| "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY. | |
