Regulation of the Activity in the p53 Family Depends on the Organization of the Transactivation Domain.
Histone acetyltransferase p300,Tumor protein 63
p300 HAT,E1A-associated protein p300,Histone butyryltransferase p300,Histone crotonyltransferase p300,Protein propionyltransferase p300,p63,Chronic ulcerative stomatitis protein,CUSP,Keratinocyte transcription factor KET,Transformation-related protein 63,TP63,Tumor protein p73-like,p73L,p40,p51
ATQSPGDSRRLSIQRAIQSLVHAAQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALAAYHAKHCQENKCP VPFCLNIKQKGTIEGRGNEFLSPEVFQHIWDFLEQPISSVQPID
structures with the least restraint violations
Fusion construct of p300 Taz2 and the transactivation domain of p63
1200 mM [U-13C; U-15N] Fusion construct of p300 Taz2 and the transactivation domain of p63, 25 mM MES, 200 mM NaCl, 0.5 mM TCEP, 95% H2O/5% D2O
Luginbuhl, Guntert, Billeter and Wuthrich
T. D. Goddard and D. G. Kneller, SPARKY 3, University of California, San Francisco
p300, CREB Binding protein, p53 family, p63, p73, ANTITUMOR PROTEIN
ATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCP VPFCLNIKQK