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Primary Information | |
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| BoMiProt ID | Bomi715 |
| Protein Name | ATP-dependent RNA helicase DDX19A |
| Organism | Bos taurus |
| Uniprot ID | Q3ZBV2 |
| Milk Fraction | Exosome |
| Ref Sequence ID | NP_001029743.1 |
| Aminoacid Length | 478 |
| Molecular Weight | 53986 |
| FASTA Sequence | Download |
| Gene Name | DDX19A |
| Gene ID | 529929 |
| Protein Existence Status | Reveiwed:Experimental evidence at transcript level |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | have ubiquitous location and function within the cell |
| Protein Function | RNA-binding proteins resolve secondary and tertiary RNA structures in an active manner, in some cases enzymatic activity is coupled to the hydrolysis of ATP; closely related to DNA helicases; essential players in cell homeostasis; suitable to complex functions, participating in tangled regulatory mechanisms; might be involved in protein-protein interactions and probably could be important factors modulating their substrate specificity and functional activity. DEAD-box RNA helicases constitute the largest family of RNA helicases and are involved in many aspects of RNA metabolism. |
| Biochemical Properties | RNA helicases are included in five of the six nucleic acid helicase superfamilies; RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins |
| PTMs | N6-acetylation at Lysine,Phosphorylation at Serine,Isopeptide bond formation,Ubl Conjugation |
| Significance of PTMs | Phosphorylated by ATM kinase; phosphorylation is increased in response to the factor of ionizing radiation. |
| Linking IDs | Bomi54 |
| Bibliography | 1. Takahasi, K., Yoneyama, M., Nishihori, T., Hirai, R., Kumeta, H., Narita, R., … Fujita, T. (2008). Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses. Molecular Cell, 29(4), 428–440. https://doi.org/10.1016/j.molcel.2007.11.028. 2. Edgcomb, S. P., Carmel, A. B., Naji, S., Ambrus-Aikelin, G., Reyes, J. R., Saphire, A. C. S., … Williamson, J. R. (2012). DDX1 is an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. Journal of Molecular Biology, 415(1), 61–74. https://doi.org/10.1016/j.jmb.2011.10.032. 3.Ishaq M, Ma L, Wu X, Mu Y, Pan J, Hu J, Hu T, Fu Q, Guo D. The DEAD-box RNA helicase DDX1 interacts with RelA and enhances nuclear factor kappaB-mediated transcription. J Cell Biochem. 2009 Feb 1;106(2):296-305. doi: 10.1002/jcb.22004. PMID: 19058135. |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
| Predicted Disorder Regions | (31-55) |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |