EAF family

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]

EAF
Identifiers
SymbolEAF
PfamPF09816
InterProIPR027093
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

References
  1. 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.
  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
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