EAF family

Last updated
EAF
Identifiers
SymbolEAF
Pfam PF09816
InterPro IPR027093
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In molecular biology, the EAF family of proteins act as transcriptional transactivators of ELL and ELL2 RNA Polymerase II (Pol II) transcriptional elongation factors. [1] [2] [3] EAF proteins form a stable heterodimer complex with ELL proteins to facilitate the binding of RNA polymerase II to activate transcription elongation. ELL and EAF1 are components of Cajal bodies, which have a role in leukemogenesis. [2] EAF1 also has the capacity to interact with ELL1 and ELL2. The N terminus of approx 120 of EAF1 has a region of high serine, aspartic acid, and glutamic acid residues. [1] [4]

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References

  1. 1 2 Simone F, Polak PE, Kaberlein JJ, Luo RT, Levitan DA, Thirman MJ (July 2001). "EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein". Blood. 98 (1): 201–9. doi:10.1182/blood.V98.1.201. PMID   11418481. S2CID   2577367.
  2. 1 2 Polak PE, Simone F, Kaberlein JJ, Luo RT, Thirman MJ (April 2003). "ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia". Mol. Biol. Cell. 14 (4): 1517–28. doi:10.1091/mbc.E02-07-0394. PMC   153119 . PMID   12686606.
  3. Kong SE, Banks CA, Shilatifard A, Conaway JW, Conaway RC (July 2005). "ELL-associated factors 1 and 2 are positive regulators of RNA polymerase II elongation factor ELL". Proc. Natl. Acad. Sci. U.S.A. 102 (29): 10094–8. Bibcode:2005PNAS..10210094K. doi: 10.1073/pnas.0503017102 . PMC   1177379 . PMID   16006523.
  4. Banks CA, Kong SE, Spahr H, Florens L, Martin-Brown S, Washburn MP, Conaway JW, Mushegian A, Conaway RC (February 2007). "Identification and Characterization of a Schizosaccharomyces pombe RNA Polymerase II Elongation Factor with Similarity to the Metazoan Transcription Factor ELL". J. Biol. Chem. 282 (8): 5761–9. doi: 10.1074/jbc.M610393200 . PMID   17150956.
This article incorporates text from the public domain Pfam and InterPro: IPR019194