TRRAP is an
adaptor protein, which is found in various multiprotein
chromatin complexes with
histone acetyltransferase activity (HAT), which in turn is responsible for
epigenetictranscription activation. TRRAP has a central role in
MYC (c-Myc) transcription activation, and also participates in cell transformation by MYC. It is required for p53/
TP53-,
E2F1-, and
E2F4-mediated transcription activation. It is also involved in transcription activation mediated by the
adenovirus E1A, a viral
oncoprotein that deregulates transcription of key genes.[7]
TRRAP is also required for the
mitotic checkpoint and normal
cell cycle progression. The
MRN complex (composed of
MRE11,
RAD50, and
NBS1) is involved in the detection and repair of DNA
double-strand breaks (DSBs). TRRAP associates with the MRN complex and when TRRAP is removed, the complex shows reduced cDNA end-joining activity. Hence, TRRAP may function as a link between DSB repair and chromatin remodeling.[8][9]
Interactions
Transformation/transcription domain-associated protein has been shown to
interact with:
Cavusoglu N, Brand M, Tora L, Van Dorsselaer A (2003). "Novel subunits of the TATA binding protein free TAFII-containing transcription complex identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry following one-dimensional gel electrophoresis". Proteomics. 3 (2): 217–23.
doi:
10.1002/pmic.200390030.
PMID12601814.
S2CID6035986.
TRRAP is an
adaptor protein, which is found in various multiprotein
chromatin complexes with
histone acetyltransferase activity (HAT), which in turn is responsible for
epigenetictranscription activation. TRRAP has a central role in
MYC (c-Myc) transcription activation, and also participates in cell transformation by MYC. It is required for p53/
TP53-,
E2F1-, and
E2F4-mediated transcription activation. It is also involved in transcription activation mediated by the
adenovirus E1A, a viral
oncoprotein that deregulates transcription of key genes.[7]
TRRAP is also required for the
mitotic checkpoint and normal
cell cycle progression. The
MRN complex (composed of
MRE11,
RAD50, and
NBS1) is involved in the detection and repair of DNA
double-strand breaks (DSBs). TRRAP associates with the MRN complex and when TRRAP is removed, the complex shows reduced cDNA end-joining activity. Hence, TRRAP may function as a link between DSB repair and chromatin remodeling.[8][9]
Interactions
Transformation/transcription domain-associated protein has been shown to
interact with:
Cavusoglu N, Brand M, Tora L, Van Dorsselaer A (2003). "Novel subunits of the TATA binding protein free TAFII-containing transcription complex identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry following one-dimensional gel electrophoresis". Proteomics. 3 (2): 217–23.
doi:
10.1002/pmic.200390030.
PMID12601814.
S2CID6035986.