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ASXL3 binds BAP1. 20 / 21
1 6 | 6 7
biogrid
No evidence text available
33961781
sparser
"Our in vitro analysis indicates that also ASXL3 can bind and activate BAP1, which is not surprising in the light of the high sequence similarity between the DEUBAD domains in the ASXL family."
26739236
biogrid
No evidence text available
32669118
reach
"Mechanistically, the chromatin bound ASXL3 functions as an adaptor protein, which directly connects BRD4 to the BAP1/ASXL3 complex and maintains chromatin occupancy of the functional BAP1/ASXL3/BRD4 epigenetic axis at active enhancers (20)."
34341073
biogrid
No evidence text available
32669118
signor
"We report a critical link between BAP1 complex and BRD4, which is bridged by the physical interaction between ASXL3 and BRD4 in an SCLC subtype (SCLC-A), which expresses a high level of ASCL1. We further showed that ASXL3 functions as an adaptor protein, which directly interacts with BRD4's extra-terminal (ET) domain via a novel BRD4 binding motif (BBM), and maintains chromatin occupancy of BRD4 to active enhancers."
32669118
biogrid
No evidence text available
26647312
biogrid
No evidence text available
26647312
reach
"ASXL3 interacts with BAP1, a ubiquitin terminal hydroxylase and removes the mono-ubiquitin (Ub1) from the H2AK119Ub1 [XREF_BIBR]."
28785287
reach
"We found that ASXL3 interacts with BAP1, a hydrolase that removes mono-ubiquitin from histone H2A lysine 119 (H2AK119Ub1) as a component of the Polycomb repressive deubiquitination (PR-DUB) complex."
26647312
reach
"While ASXL1 and ASXL2 were known to interact with BAP1 from proteomics studies XREF_BIBR XREF_BIBR, ASXL3 was not detected as a BAP1 binding partner, possibly because of the low levels of BAP1 and ASXL3 complexes in cells."
26739236
sparser
"ASXL3 interacts with BAP1 which functions as a component of the Polycomb repressive deubiquitination (PR‐DUB) complex, playing a role in chromatin remodelling on transcriptional regulation (Srivastava et al.,  xref )."
35276034
reach
"Our in vitro analysis indicates that also ASXL3 can bind and activate BAP1, which is not surprising in the light of the high sequence similarity between the DEUBAD domains in the ASXL family."
26739236
reach
"It suggests that there may be a functional association between BAP1 and ASXL3 in cells and further cell based work is required to shed more light on this issue."
26739236
sparser
"ASXL3 interacts with BAP1, a ubiquitin terminal hydroxylase and removes the mono-ubiquitin (Ub1) from the H2AK119Ub1 [ xref ]."
28785287
biogrid
No evidence text available
| DOI
sparser
"ASXL3 interacts with BAP1 , forming a key component of the polycomb repressive deubiquitination (PR-DUB) complex, which functions to remove the monoubiquitin from lysine-119 of histone H2A, playing a [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
33242595
sparser
"We found that ASXL3 interacts with BAP1, a hydrolase that removes mono-ubiquitin from histone H2A lysine 119 (H2AK119Ub1) as a component of the Polycomb repressive deubiquitination (PR-DUB) complex."
26647312
sparser
"Interestingly, the truncated ASXL3 protein interacts with BAP1 protein ( xref )."
32132929
sparser
"ASXL3 interacts directly with BAP1, a core component of the Polycomb repressive deubiquitination (PRDUB) complex that is essential for transcriptional regulation ( xref ; xref )."
41659201