This entry represents the N-terminal domain of ELL-associated factor (Eaf) proteins, which act as transcriptional transactivators of ELL and ELL2 RNA Polymerase II (Pol II) transcriptional elongation factors [, , , ]. 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 []. 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 [, ].
This entry represents the ELL-associated factor (Eaf) family of proteins. They interact with ELL and ELL2, which are RNA polymerase II elongation factors. 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 [].
This entry includes PAX-interacting protein 1 (PTIP or Swift) and chromatin modification-related protein eaf1 (from Aspergillus fumigatus). PTIP is involved in the DNA damage response and is an adaptor protein for the ATM/ATR kinases. PTIP contains five BRCT domains with which it interacts with the activation domain of the transcription factor Pax2 []. Knockout of PTIP prevent ubiquitination of proliferating cell nuclear antigen (PCNA), and monoubiquitination of PCNA enables translesion synthesis by specialized DNA polymerases to replicate damaged DNA []. Cells without PTIP are unable to progress through mitosis []. PTIP is a component of the MLL2/MLL3 complex [], but a PTIP-PA1 subcomplex functions independently of the MLL3/MLL4 complex to mediate transcription during class switch recombination, important for generating antibody diversity []. In Saccharomyces cerevisiae, EAF1 is a component of the NuA4 histone acetyltransferase complex involved in acetylation of nucleosomal histone H4 and H2A [].
The helicase/SANT-associated (HSA) domain is found in eukaryotic proteins, including Helicase SRCAP/p400/DOM [], Probable global transcription activator SNF2L2/brahma-homologue and Chromatin modification-related protein EAF1 []. While each family has the core sequences that define the HSA domain, they each also have additional sequences that distinguish these families from one another. For example, the sequence HWDY(L/C)EEEM(Q/V) is found in the SRCAP/p400/DOM family, whereas the sequence HQE(Y/F)LNSILQ is found in the SNF2 /brahma family [].HSA was initially predicted to be a DNA-binding domain [], but it was later reported to be responsible for the binding to nuclear actin-related proteins (ARPs) and actin []. In addition to the SANT and helicase domains, the HSA domain is also found in association with the bromo domain [].
