[HTML][HTML] Ptip associates with mll3-and mll4-containing histone h3 lysine 4 methyltransferase complex*♦
PTIP, a protein with tandem BRCT domains, has been implicated in DNA damage response.
However, its normal cellular functions remain unclear. Here we show that while ectopically
expressed PTIP is capable of interacting with DNA damage response proteins including
53BP1, endogenous PTIP, and a novel protein PA1 are both components of a Set1-like
histone methyltransferase (HMT) complex that also contains ASH2L, RBBP5, WDR5, hDPY-
30, NCOA6, SET domain-containing HMTs MLL3 and MLL4, and substoichiometric amount …
However, its normal cellular functions remain unclear. Here we show that while ectopically
expressed PTIP is capable of interacting with DNA damage response proteins including
53BP1, endogenous PTIP, and a novel protein PA1 are both components of a Set1-like
histone methyltransferase (HMT) complex that also contains ASH2L, RBBP5, WDR5, hDPY-
30, NCOA6, SET domain-containing HMTs MLL3 and MLL4, and substoichiometric amount …