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- eIF-4B、eukaryotic initiation factor-4B、eukaryotic translation initiation factor 4B
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/01/07 14:26:20」(JST)
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Eukaryotic translation initiation factor 4B |
PDB rendering based on 1wi8.
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Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1WI8, 2J76
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Identifiers |
Symbols |
EIF4B ; EIF-4B; PRO1843 |
External IDs |
OMIM: 603928 MGI: 95304 HomoloGene: 83162 GeneCards: EIF4B Gene |
Gene ontology |
Molecular function |
• nucleotide binding
• RNA binding
• translation initiation factor activity
• protein binding
• poly(A) RNA binding
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Cellular component |
• cytosol
• eukaryotic translation initiation factor 4F complex
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Biological process |
• nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
• nuclear-transcribed mRNA poly(A) tail shortening
• translation
• translational initiation
• regulation of translational initiation
• insulin receptor signaling pathway
• gene expression
• cellular protein metabolic process
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
1975 |
75705 |
Ensembl |
ENSG00000063046 |
ENSMUSG00000058655 |
UniProt |
P23588 |
Q8BGD9 |
RefSeq (mRNA) |
NM_001300821 |
NM_145625 |
RefSeq (protein) |
NP_001287750 |
NP_663600 |
Location (UCSC) |
Chr 12:
53.01 – 53.04 Mb |
Chr 15:
102.07 – 102.1 Mb |
PubMed search |
[1] |
[2] |
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Eukaryotic translation initiation factor 4B is a protein that in humans is encoded by the EIF4B gene.[1]
Contents
- 1 Interactions
- 2 References
- 3 External links
- 4 Further reading
Interactions
EIF4B has been shown to interact with EIF3A.[2]
References
- ^ "Entrez Gene: EIF4B eukaryotic translation initiation factor 4B".
- ^ Méthot N, Song MS, Sonenberg N (Oct 1996). "A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3". Mol. Cell. Biol. 16 (10): 5328–34. PMC 231531. PMID 8816444.
External links
- Cap-dependent translation initiation from Nature Reviews Microbiology. A good image and overview of the function of initiation factors
Further reading
- van Heugten HA, Kasperaitis MA, Thomas AA, Voorma HO (1991). "Evidence that eukaryotic initiation factor (eIF) 2 is a cap-binding protein that stimulates cap recognition by eIF-4B and eIF-4F". J. Biol. Chem. 266 (11): 7279–84. PMID 2016328.
- Milburn SC, Hershey JW, Davies MV, Kelleher K, Kaufman RJ (1990). "Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif". EMBO J. 9 (9): 2783–90. PMC 551988. PMID 2390971.
- Howe JG, Hershey JW (1984). "Translational initiation factor and ribosome association with the cytoskeletal framework fraction from HeLa cells". Cell 37 (1): 85–93. doi:10.1016/0092-8674(84)90303-9. PMID 6722878.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Méthot N, Pause A, Hershey JW, Sonenberg N (1994). "The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence". Mol. Cell. Biol. 14 (4): 2307–16. doi:10.1128/mcb.14.4.2307. PMC 358597. PMID 8139536.
- Naranda T, Strong WB, Menaya J, Fabbri BJ, Hershey JW (1994). "Two structural domains of initiation factor eIF-4B are involved in binding to RNA". J. Biol. Chem. 269 (20): 14465–72. PMID 8182051.
- Méthot N, Song MS, Sonenberg N (1996). "A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3". Mol. Cell. Biol. 16 (10): 5328–34. PMC 231531. PMID 8816444.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Richter NJ, Rogers GW, Hensold JO, Merrick WC (1999). "Further biochemical and kinetic characterization of human eukaryotic initiation factor 4H". J. Biol. Chem. 274 (50): 35415–24. doi:10.1074/jbc.274.50.35415. PMID 10585411.
- Bushell M, Wood W, Clemens MJ, Morley SJ (2000). "Changes in integrity and association of eukaryotic protein synthesis initiation factors during apoptosis". Eur. J. Biochem. 267 (4): 1083–91. doi:10.1046/j.1432-1327.2000.01101.x. PMID 10672017.
- Bushell M, Wood W, Carpenter G, Pain VM, Morley SJ, Clemens MJ (2001). "Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages". J. Biol. Chem. 276 (26): 23922–8. doi:10.1074/jbc.M100384200. PMID 11274152.
- Fleming K, Ghuman J, Yuan X, Simpson P, Szendröi A, Matthews S, Curry S (2003). "Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B". Biochemistry 42 (30): 8966–75. doi:10.1021/bi034506g. PMID 12885229.
- Raught B, Peiretti F, Gingras AC, Livingstone M, Shahbazian D, Mayeur GL, Polakiewicz RD, Sonenberg N, Hershey JW (2004). "Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases". EMBO J. 23 (8): 1761–9. doi:10.1038/sj.emboj.7600193. PMC 394247. PMID 15071500.
- Doepker RC, Hsu WL, Saffran HA, Smiley JR (2004). "Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H". J. Virol. 78 (9): 4684–99. doi:10.1128/JVI.78.9.4684-4699.2004. PMC 387725. PMID 15078951.
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
- Shahbazian D, Roux PP, Mieulet V, Cohen MS, Raught B, Taunton J, Hershey JW, Blenis J, Pende M, Sonenberg N (2006). "The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity". EMBO J. 25 (12): 2781–91. doi:10.1038/sj.emboj.7601166. PMC 1500846. PMID 16763566.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
PDB gallery
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1wi8: Solution structure of the RNA binding domain of eukaryotic initiation factor 4B
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English Journal
- MicroRNA‑216a inhibits the growth and metastasis of oral squamous cell carcinoma by targeting eukaryotic translation initiation factor 4B.
- Li L1, Ma HQ1.
- Molecular medicine reports.Mol Med Rep.2015 Aug;12(2):3156-62. doi: 10.3892/mmr.2015.3761. Epub 2015 May 8.
- There is increasing evidence to suggest that microRNAs (miRNAs; miRs) are involved in the development of oral squamous cell carcinoma (OSCC). miR‑216a has been identified as being involved in tumorigenesis, however, the mechanisms of miR‑216a in various types of cancer, either as a tumor suppres
- PMID 25955794
- ORF45-Mediated Prolonged c-Fos Accumulation Accelerates Viral Transcription during the Late Stage of Lytic Replication of Kaposi's Sarcoma-Associated Herpesvirus.
- Li X1, Du S2, Avey D3, Li Y2, Zhu F3, Kuang E4.
- Journal of virology.J Virol.2015 Jul 1;89(13):6895-906. doi: 10.1128/JVI.00274-15. Epub 2015 Apr 22.
- Kaposi's sarcoma-associated herpesvirus (KSHV) encodes multiple viral proteins that activate extracellular signal-regulated kinase (ERK)-mitogen-activated protein kinase (MAPK) cascades. One of these viral proteins, ORF45, mediates sustained ERK-p90 ribosomal S6 kinase (RSK) activation during KSHV l
- PMID 25903346
- Genetic ablation of ataxin-2 increases several global translation factors in their transcript abundance but decreases translation rate.
- Fittschen M1, Lastres-Becker I, Halbach MV, Damrath E, Gispert S, Azizov M, Walter M, Müller S, Auburger G.
- Neurogenetics.Neurogenetics.2015 Jul;16(3):181-92. doi: 10.1007/s10048-015-0441-5. Epub 2015 Feb 27.
- Spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS) are neurodegenerative disorders, caused or modified by an unstable CAG-repeat expansion in the SCA2 gene, which encodes a polyglutamine (polyQ) domain expansion in ataxin-2 (ATXN2). ATXN2 is an RNA-binding protein and inter
- PMID 25721894
Japanese Journal
- Pim Kinase Substrate Identification and Specificity
- Peng Charline,Knebel Axel,Morrice Nick A. [他],LI Xiang,BARRINGER Kevin,LI Jun,JAKES Scott,WERNEBURG Brian,WANG Lian
- The journal of biochemistry 141(3), 353-362, 2007-03-01
- NAID 10020100637
- The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity
Related Links
- "A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3." Methot N., Song M.S., Sonenberg N. Mol. Cell. Biol. 16:5328-5334] [] ...
- Complete information for EIF4B gene (Protein Coding), Eukaryotic Translation Initiation Factor 4B, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium ... A ...
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