Biology:ELL (gene)

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

RNA polymerase II elongation factor ELL is an enzyme that in humans is encoded by the ELL gene.

Interactions

ELL (gene) has been shown to interact with P53.

Further reading

• "Two cellular proteins that bind to wild-type but not mutant p53.". Proc. Natl. Acad. Sci. U.S.A. 91 (13): 6098–102. 1994. doi:10.1073/pnas.91.13.6098. PMID 8016121. Bibcode: 1994PNAS...91.6098I. 
• "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• "Structure and function of RNA polymerase II elongation factor ELL. Identification of two overlapping ELL functional domains that govern its interaction with polymerase and the ternary elongation complex". J. Biol. Chem. 272 (35): 22355–63. 1997. doi:10.1074/jbc.272.35.22355. PMID 9268387. 
• "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• "Identification and purification of the Holo-ELL complex. Evidence for the presence of ELL-associated proteins that suppress the transcriptional inhibitory activity of ELL". J. Biol. Chem. 273 (18): 11212–7. 1998. doi:10.1074/jbc.273.18.11212. PMID 9556611. 
• "The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor". Genes Dev. 12 (19): 2992–6. 1998. doi:10.1101/gad.12.19.2992. PMID 9765201. 
• "Physical interaction and functional antagonism between the RNA polymerase II elongation factor ELL and p53". J. Biol. Chem. 274 (24): 17003–10. 1999. doi:10.1074/jbc.274.24.17003. PMID 10358050. 
• "Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II". J. Biol. Chem. 274 (31): 21981–5. 1999. doi:10.1074/jbc.274.31.21981. PMID 10419521. 
• "hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation". Mol. Cell. Biol. 19 (10): 6833–44. 2000. doi:10.1128/MCB.19.10.6833. PMID 10490622. 
• "Retrovirus-mediated gene transfer of MLL-ELL transforms primary myeloid progenitors and causes acute myeloid leukemias in mice". Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10984–9. 2000. doi:10.1073/pnas.190167297. PMID 10995463. Bibcode: 2000PNAS...9710984L. 
• "EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein". Blood 98 (1): 201–9. 2001. doi:10.1182/blood.V98.1.201. PMID 11418481. 
• "The elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELL-induced leukemogenesis". Mol. Cell. Biol. 21 (16): 5678–87. 2001. doi:10.1128/MCB.21.16.5678-5687.2001. PMID 11463848. 
• "ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with alternative ELL binding properties". Blood 101 (6): 2355–62. 2003. doi:10.1182/blood-2002-06-1664. PMID 12446457. 
• "ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia". Mol. Biol. Cell 14 (4): 1517–28. 2003. doi:10.1091/mbc.E02-07-0394. PMID 12686606. 
• "Molecular basis of p53 functional inactivation by the leukemic protein MLL-ELL". Mol. Cell. Biol. 23 (12): 4230–46. 2003. doi:10.1128/MCB.23.12.4230-4246.2003. PMID 12773566.